{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,20]],"date-time":"2026-09-20T03:06:37Z","timestamp":1789873597773,"version":"4.0.1"},"reference-count":319,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100020582","name":"National Institute of Pharmaceutical Education and Research, Raebareli","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100020582","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100020703","name":"Department of Pharmaceutical Sciences, St. John's University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100020703","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100023983","name":"Babasaheb Bhimrao Ambedkar University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100023983","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["International Journal of Biological Macromolecules"],"published-print":{"date-parts":[[2025,5]]},"DOI":"10.1016\/j.ijbiomac.2025.142158","type":"journal-article","created":{"date-parts":[[2025,3,17]],"date-time":"2025-03-17T03:51:38Z","timestamp":1742183498000},"page":"142158","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":23,"special_numbering":"P3","title":["Harnessing marine antimicrobial peptides for novel therapeutics: A deep dive into ocean-derived bioactives"],"prefix":"10.1016","volume":"307","author":[{"given":"Kunal Agam","family":"Kanaujia","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Suraj","family":"Wagh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Giriraj","family":"Pandey","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vivek","family":"Phatale","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pooja","family":"Khairnar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tejaswini","family":"Kolipaka","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"P.S.","family":"Rajinikanth","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shubhini A.","family":"Saraf","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Saurabh","family":"Srivastava","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shailendra","family":"Kumar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ijbiomac.2025.142158_bb0005","doi-asserted-by":"crossref","DOI":"10.1111\/jfbc.14348","article-title":"Plant derived antimicrobial peptides: mechanism of target, isolation techniques, sources and pharmaceutical applications","volume":"46","author":"Sharma","year":"2022","journal-title":"J. Food Biochem."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0010","first-page":"183291","article-title":"Binding of an antimicrobial peptide to bacterial cells: interaction with different species, strains and cellular components","volume":"2020","author":"Savini","year":"1862","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0015","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2023.128452","article-title":"Supramolecular self-assembled peptide-engineered nanofibers: a propitious proposition for cancer therapy","volume":"256","author":"Pandey","year":"2024","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0020","doi-asserted-by":"crossref","DOI":"10.1016\/j.colsurfb.2022.112693","article-title":"Antimicrobial peptides and their potential application in antiviral coating agents","volume":"217","author":"Freitas","year":"2022","journal-title":"Colloids Surf. B: Biointerfaces"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0025","series-title":"Biosynthesis of Peptide Antibiotics and Innate Immunity","first-page":"17","author":"Ajesh","year":"2023"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0030","doi-asserted-by":"crossref","first-page":"1407","DOI":"10.1080\/17460441.2023.2157402","article-title":"Tachyplesin I and its derivatives: a pharmaco-chemical perspective on their antimicrobial and antitumor potential","volume":"17","author":"Lu","year":"2022","journal-title":"Expert Opin. Drug Discov."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0035","doi-asserted-by":"crossref","first-page":"4437","DOI":"10.1111\/ijfs.17248","article-title":"The structure\u2013activity relationship of marine peptides: a review","volume":"59","author":"Ashaolu","year":"2024","journal-title":"Int. J. Food Sci. Technol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0040","doi-asserted-by":"crossref","DOI":"10.3389\/fchem.2021.691532","article-title":"Antimicrobial peptides and proteins: from Nature\u2019s reservoir to the laboratory and beyond","volume":"9","author":"Sarkar","year":"2021","journal-title":"Front. Chem."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0045","doi-asserted-by":"crossref","first-page":"503","DOI":"10.3390\/md21100503","article-title":"Marine invertebrate antimicrobial peptides and their potential as novel peptide antibiotics","volume":"21","author":"Guryanova","year":"2023","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0050","doi-asserted-by":"crossref","DOI":"10.3389\/fmars.2022.1112595","article-title":"Antimicrobial peptides from marine animals: sources, structures, mechanisms and the potential for drug development","volume":"9","author":"Wang","year":"2023","journal-title":"Front. Mar. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0055","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1016\/j.tifs.2021.08.017","article-title":"Bioactive peptides derived from marine sources: biological and functional properties","volume":"119","author":"Cunha","year":"2022","journal-title":"Trends Food Sci. Technol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0060","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2023.115377","article-title":"Antimicrobial peptides: structure, mechanism, and modification","volume":"255","author":"Chen","year":"2023","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0065","series-title":"Antimicrobial Peptides of Multicellular Organisms: My Perspective","first-page":"3","author":"Zasloff","year":"2019"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0070","doi-asserted-by":"crossref","first-page":"25","DOI":"10.2174\/1568026615666150703121700","article-title":"Antimicrobial peptide structure and mechanism of action: a focus on the role of membrane structure","volume":"16","author":"Lee","year":"2015","journal-title":"Curr. Top. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0075","doi-asserted-by":"crossref","first-page":"1937","DOI":"10.3390\/ani11071937","article-title":"Antimicrobial peptides from black soldier Fly (Hermetia illucens) as potential antimicrobial factors representing an alternative to antibiotics in livestock farming","volume":"11","author":"Xia","year":"2021","journal-title":"Animals"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0080","doi-asserted-by":"crossref","first-page":"290","DOI":"10.3390\/md21050290","article-title":"Antimicrobial peptides from photosynthetic marine organisms with potential application in aquaculture","volume":"21","author":"Garc\u00eda-Beltr\u00e1n","year":"2023","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0085","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1080\/00071668.2021.1919993","article-title":"Antimicrobial peptides as an alternative to relieve antimicrobial growth promoters in poultry","volume":"62","author":"Nazeer","year":"2021","journal-title":"Br. Poult. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0090","doi-asserted-by":"crossref","DOI":"10.3389\/fmars.2021.667764","article-title":"Marine organisms as a rich source of biologically active peptides","volume":"8","author":"Macedo","year":"2021","journal-title":"Front. Mar. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0095","doi-asserted-by":"crossref","first-page":"301","DOI":"10.3390\/md20050301","article-title":"Preclinical development of Seriniquinones as selective Dermcidin modulators for the treatment of melanoma","volume":"20","author":"Hirata","year":"2022","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0100","doi-asserted-by":"crossref","first-page":"1538","DOI":"10.1128\/AAC.02427-13","article-title":"Use of the antimicrobial peptide Pardaxin (GE33) to protect against methicillin-resistant Staphylococcus aureus infection in mice with skin injuries","volume":"58","author":"Huang","year":"2014","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0105","doi-asserted-by":"crossref","first-page":"505","DOI":"10.3390\/md21100505","article-title":"Genome-wide identification of Trachinotus ovatus antimicrobial peptides and their immune response against two pathogen challenges","volume":"21","author":"Liang","year":"2023","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0110","doi-asserted-by":"crossref","first-page":"40329","DOI":"10.18632\/oncotarget.9612","article-title":"Targeting FOSB with a cationic antimicrobial peptide, TP4, for treatment of triple-negative breast cancer","volume":"7","author":"Ting","year":"2016","journal-title":"Oncotarget"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0115","doi-asserted-by":"crossref","first-page":"D1087","DOI":"10.1093\/nar\/gkv1278","article-title":"APD3: the antimicrobial peptide database as a tool for research and education","volume":"44","author":"Wang","year":"2016","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0120","doi-asserted-by":"crossref","first-page":"86","DOI":"10.2174\/138920109787048625","article-title":"Marine sponges: potential sources of new antimicrobial drugs","volume":"10","author":"Laport","year":"2009","journal-title":"Curr. Pharm. Biotechnol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0125","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/j.marenvres.2016.05.002","article-title":"Marine microorganisms as a promising and sustainable source of bioactive molecules","volume":"128","author":"Romano","year":"2017","journal-title":"Mar. Environ. Res."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0130","doi-asserted-by":"crossref","first-page":"636","DOI":"10.1016\/j.chembiol.2013.04.011","article-title":"Metagenomic approaches for exploiting uncultivated Bacteria as a resource for novel biosynthetic enzymology","volume":"20","author":"Wilson","year":"2013","journal-title":"Chem. Biol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0135","doi-asserted-by":"crossref","unstructured":"Y. Bashir, S. Pradeep Singh, B. Kumar Konwar, Metagenomics: An application based perspective, Chin. J. Biol. 2014 (2014) 1\u20137. doi:https:\/\/doi.org\/10.1155\/2014\/146030.","DOI":"10.1155\/2014\/146030"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0140","doi-asserted-by":"crossref","first-page":"208","DOI":"10.3390\/md20030208","article-title":"Exploring marine as a rich source of bioactive peptides: challenges and opportunities from marine pharmacology","volume":"20","author":"Ahmed","year":"2022","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0145","doi-asserted-by":"crossref","DOI":"10.3389\/fmars.2021.667764","article-title":"Marine organisms as a rich source of biologically active peptides","volume":"8","author":"Macedo","year":"2021","journal-title":"Front. Mar. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0150","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1007\/s42995-022-00132-3","article-title":"Chemical and biological diversity of new natural products from marine sponges: a review (2009\u20132018)","volume":"4","author":"Hong","year":"2022","journal-title":"Mar. Life Sci. Technol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0155","article-title":"A review on the screening methods for the discovery of natural antimicrobial peptides","author":"Yang","year":"2024","journal-title":"J. Pharm. Anal."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0160","doi-asserted-by":"crossref","first-page":"308","DOI":"10.3390\/md19060308","article-title":"Marine natural products from tunicates and their associated microbes","volume":"19","author":"Ramesh","year":"2021","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0165","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1002\/jez.b.23135","article-title":"Transcriptomic profiling of immune-associated molecules in the coelomocytes of lugworm Arenicola marina (Linnaeus, 1758)","volume":"340","author":"Stanovova","year":"2023","journal-title":"J. Exp. Zool. B Mol. Dev. Evol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0170","series-title":"Antimicrobial Peptides: Their History, Evolution, and Functional Promiscuity","first-page":"1","year":"2013"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0175","doi-asserted-by":"crossref","DOI":"10.3389\/fmars.2022.1112595","article-title":"Antimicrobial peptides from marine animals: sources, structures, mechanisms and the potential for drug development","volume":"9","author":"Wang","year":"2023","journal-title":"Front. Mar. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0180","doi-asserted-by":"crossref","first-page":"7698","DOI":"10.1021\/acs.est.3c01664","article-title":"Antimicrobial peptides in the global microbiome: biosynthetic genes and resistance determinants","volume":"57","author":"Chen","year":"2023","journal-title":"Environ. Sci. Technol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0185","doi-asserted-by":"crossref","first-page":"1608","DOI":"10.1111\/2041-210X.13894","article-title":"Synthetic microbial consortia with programmable ecological interactions","volume":"13","author":"Li","year":"2022","journal-title":"Methods Ecol. Evol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0190","doi-asserted-by":"crossref","first-page":"12679","DOI":"10.1038\/s41598-020-69126-4","article-title":"Transcriptome profiling and in silico detection of the antimicrobial peptides of red king crab Paralithodes camtschaticus","volume":"10","author":"Yakovlev","year":"2020","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0195","doi-asserted-by":"crossref","first-page":"4691","DOI":"10.1021\/acs.jcim.0c00841","article-title":"IAMPE: NMR-assisted computational prediction of antimicrobial peptides","volume":"60","author":"Kavousi","year":"2020","journal-title":"J. Chem. Inf. Model."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0200","doi-asserted-by":"crossref","DOI":"10.1016\/j.compbiomed.2022.106311","article-title":"Target-AMP: computational prediction of antimicrobial peptides by coupling sequential information with evolutionary profile","volume":"151","author":"Jan","year":"2022","journal-title":"Comput. Biol. Med."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0205","doi-asserted-by":"crossref","DOI":"10.3389\/fmars.2021.742188","article-title":"Shifting baselines to thresholds: reframing exploitation in the marine environment","volume":"8","author":"Atmore","year":"2021","journal-title":"Front. Mar. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0210","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2024.135823","article-title":"A comprehensive review of marine sponge metabolites, with emphasis on Neopetrosia sp","volume":"280","author":"Barzkar","year":"2024","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0215","doi-asserted-by":"crossref","first-page":"537","DOI":"10.3390\/ijms25010537","article-title":"Animal microbiomes as a source of novel antibiotic-producing strains","volume":"25","author":"Baranova","year":"2023","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0220","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1007\/s11274-024-04120-w","article-title":"Biofilm-forming bacteria associated with corals secrete melanin with UV-absorption properties","volume":"40","author":"Ashraf","year":"2024","journal-title":"World J. Microbiol. Biotechnol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0225","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1111\/raq.12314","article-title":"Antimicrobial peptides from fish: beyond the fight against pathogens","volume":"12","author":"Valero","year":"2020","journal-title":"Rev. Aquac."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0230","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1007\/s13197-022-05585-z","article-title":"Identification and characterization of antimicrobial peptide (AMP) candidate from Gonggong Sea snail (Leavistrombus turturella) extract","volume":"60","author":"Viruly","year":"2023","journal-title":"J. Food Sci. Technol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0235","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1016\/j.ijbiomac.2021.09.082","article-title":"Diversity of insect antimicrobial peptides and proteins - a functional perspective: a review","volume":"191","author":"Eleftherianos","year":"2021","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0240","doi-asserted-by":"crossref","first-page":"1451","DOI":"10.1007\/s10989-019-09946-9","article-title":"Antimicrobial Peptides (AMPs): Roles","volume":"26","author":"Seyfi","year":"2020","journal-title":"Functions and Mechanism of Action, Int. J. Pept. Res. Ther."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0245","doi-asserted-by":"crossref","first-page":"503","DOI":"10.3390\/md21100503","article-title":"Marine invertebrate antimicrobial peptides and their potential as novel peptide antibiotics","volume":"21","author":"Guryanova","year":"2023","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0250","doi-asserted-by":"crossref","first-page":"48","DOI":"10.3390\/md14030048","article-title":"Antimicrobials from cnidarians. A new perspective for anti-infective therapy?","volume":"14","author":"Mariottini","year":"2016","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0255","first-page":"91","article-title":"Piscidin","volume":"27","author":"Raju","year":"2021","journal-title":"Fish Antimicrobial Peptide: Structure, Classification, Properties, Mechanism, Gene Regulation and Therapeutical Importance, Int J Pept Res Ther"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0260","doi-asserted-by":"crossref","first-page":"37","DOI":"10.3390\/antibiotics9010037","article-title":"Molecular diversity of Mytilin-like defense peptides in Mytilidae (Mollusca, Bivalvia)","volume":"9","author":"Greco","year":"2020","journal-title":"Antibiotics"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0265","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.algal.2017.10.008","article-title":"Ulvan from Ulva armoricana (Chlorophyta) activates the PI3K\/Akt signalling pathway via TLR4 to induce intestinal cytokine production","volume":"28","author":"Berri","year":"2017","journal-title":"Algal Res."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0270","doi-asserted-by":"crossref","unstructured":"B. Krishnarjuna, C.A. MacRaild, P. Sunanda, R.A.V. Morales, S. Peigneur, J. Macrander, H.H. Yu, M. Daly, S. Raghothama, V. Dhawan, S. Chauhan, J. Tytgat, M.W. Pennington, R.S. Norton, Structure, folding and stability of a minimal homologue from Anemonia sulcata of the sea anemone potassium channel blocker ShK, Peptides (N.Y.) 99 (2018) 169\u2013178. doi:https:\/\/doi.org\/10.1016\/j.peptides.2017.10.001.","DOI":"10.1016\/j.peptides.2017.10.001"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0275","doi-asserted-by":"crossref","DOI":"10.1002\/psc.3138","article-title":"Salicylic acid influences the protease activity and posttranslation modifications of the secreted peptides in the moss <scp> Physcomitrella patens <\/scp>","volume":"25","author":"Filippova","year":"2019","journal-title":"J. Pept. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0280","first-page":"53","article-title":"Methods for the study of pericentrin in centrosome assembly and function","author":"Purohit","year":"2001","journal-title":"in"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0285","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1016\/j.molimm.2015.08.009","article-title":"Antimicrobial proteins: from old proteins, new tricks","volume":"68","author":"Smith","year":"2015","journal-title":"Mol. Immunol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0290","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/j.bbrc.2012.10.092","article-title":"Recombinant expression and solution structure of antimicrobial peptide aurelin from jellyfish Aurelia aurita","volume":"429","author":"Shenkarev","year":"2012","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0295","doi-asserted-by":"crossref","first-page":"3684","DOI":"10.3390\/foods12193684","article-title":"Tunicates as sources of high-quality nutrients and bioactive compounds for food\/feed and pharmaceutical applications: a Review","volume":"12","author":"Gao","year":"2023","journal-title":"Foods"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0300","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1016\/j.ijbiomac.2013.06.030","article-title":"Brown seaweed fucoidan: biological activity and apoptosis, growth signaling mechanism in cancer","volume":"60","author":"Senthilkumar","year":"2013","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0305","doi-asserted-by":"crossref","first-page":"1007","DOI":"10.3390\/biom10071007","article-title":"Ten-year research update Review: antiviral activities from marine organisms","volume":"10","author":"Riccio","year":"2020","journal-title":"Biomolecules"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0310","doi-asserted-by":"crossref","unstructured":"M. Zhou, T. Chen, B. Walker, C. Shaw, Pelophylaxins: Novel antimicrobial peptide homologs from the skin secretion of the Fukien gold-striped pond frog, Pelophylax plancyi fukienensis, Peptides (N.Y.) 27 (2006) 36\u201341. doi:https:\/\/doi.org\/10.1016\/j.peptides.2005.07.007.","DOI":"10.1016\/j.peptides.2005.07.007"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0315","doi-asserted-by":"crossref","first-page":"216","DOI":"10.3103\/S0891416819040062","article-title":"Search and selection of Bacteriocin-producing strains of marine Bacteria in the aquatic ecosystems of the sea of Japan","volume":"34","author":"Mikhailov","year":"2019","journal-title":"Mol. Genet. Microbiol. Virol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0320","doi-asserted-by":"crossref","first-page":"6601","DOI":"10.1007\/s00253-016-7671-9","article-title":"Fungal proteinaceous compounds with multiple biological activities","volume":"100","author":"Ng","year":"2016","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0325","series-title":"Bioactive Compounds from Marine Gorgonian Corals","first-page":"325","author":"Qi","year":"2012"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0330","doi-asserted-by":"crossref","first-page":"58","DOI":"10.3390\/md14030058","article-title":"Marine natural products from New Caledonia\u2014a Review","volume":"14","author":"Motuhi","year":"2016","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0335","first-page":"215","article-title":"Marine benthic amphipods (Amphipoda) of India: An assessment on their biodiversity","volume":"39","author":"Bhoi","year":"2023","journal-title":"Distribution and Significance, Thalassas: An International Journal of Marine Sciences"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0340","doi-asserted-by":"crossref","first-page":"612","DOI":"10.3390\/md20100612","article-title":"In vitro modulation of complement activation by therapeutically prospective analogues of the marine Polychaeta Arenicin peptides","volume":"20","author":"Krenev","year":"2022","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0345","doi-asserted-by":"crossref","first-page":"361","DOI":"10.3390\/md18070361","article-title":"Molecular and functional diversity of Crustin-like genes in the shrimp Litopenaeus vannamei","volume":"18","author":"Li","year":"2020","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0350","doi-asserted-by":"crossref","unstructured":"A. Matos, D. Dom\u00ednguez-P\u00e9rez, D. Almeida, G. Ag\u00fcero-Chapin, A. Campos, H. Os\u00f3rio, V. Vasconcelos, A. Antunes, Shotgun Proteomics of Ascidians Tunic Gives New Insights on Host\u2013Microbe Interactions by Revealing Diverse Antimicrobial Peptides, Mar. Drugs 18 (2020) 362. doi:https:\/\/doi.org\/10.3390\/md18070362.","DOI":"10.3390\/md18070362"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0355","doi-asserted-by":"crossref","first-page":"3684","DOI":"10.3390\/foods12193684","article-title":"Tunicates as sources of high-quality nutrients and bioactive compounds for food\/feed and pharmaceutical applications: a Review","volume":"12","author":"Gao","year":"2023","journal-title":"Foods"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0360","first-page":"1506","article-title":"Phycobiliproteins: structural aspects, functional characteristics, and biotechnological perspectives, Comput Struct","volume":"20","author":"Dagnino-Leone","year":"2022","journal-title":"Biotechnol. J."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0365","doi-asserted-by":"crossref","first-page":"503","DOI":"10.3390\/md21100503","article-title":"Marine invertebrate antimicrobial peptides and their potential as novel peptide antibiotics","volume":"21","author":"Guryanova","year":"2023","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0370","doi-asserted-by":"crossref","first-page":"503","DOI":"10.3390\/md21100503","article-title":"Marine invertebrate antimicrobial peptides and their potential as novel peptide antibiotics","volume":"21","author":"Guryanova","year":"2023","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0375","doi-asserted-by":"crossref","unstructured":"K. CL, M. Jeyaraman, N. Jeyaraman, S. Ramasubramanian, M. Khanna, S. Yadav, Antimicrobial effects of platelet-rich plasma and platelet-rich fibrin: a scoping Review, Cureus (2023). doi:https:\/\/doi.org\/10.7759\/cureus.51360.","DOI":"10.7759\/cureus.51360"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0380","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/S0009-3084(03)00020-3","article-title":"Lipid compounds of freshwater sponges: family Spongillidae, class Demospongiae","volume":"123","author":"Dembitsky","year":"2003","journal-title":"Chem. Phys. Lipids"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0385","doi-asserted-by":"crossref","first-page":"7546","DOI":"10.3390\/molecules27217546","article-title":"Marine antimicrobial peptides-based strategies for tackling bacterial biofilm and biofouling challenges","volume":"27","author":"Patra","year":"2022","journal-title":"Molecules"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0390","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1007\/s10989-022-10478-y","article-title":"The antiviral activity of cyclic peptides","volume":"29","author":"Chia","year":"2022","journal-title":"Int. J. Pept. Res. Ther."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0395","doi-asserted-by":"crossref","first-page":"1969","DOI":"10.3390\/md9101969","article-title":"Inducible ASABF-type antimicrobial peptide from the sponge Suberites domuncula: Microbicidal and hemolytic activity in vitro and toxic effect on Molluscs in vivo","volume":"9","author":"Wiens","year":"2011","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0400","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/j.ympev.2011.10.008","article-title":"Estimation of divergence times in cnidarian evolution based on mitochondrial protein-coding genes and the fossil record","volume":"62","author":"Park","year":"2012","journal-title":"Mol. Phylogenet. Evol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0405","doi-asserted-by":"crossref","DOI":"10.3389\/fmars.2022.1112595","article-title":"Antimicrobial peptides from marine animals: sources, structures, mechanisms and the potential for drug development","volume":"9","author":"Wang","year":"2023","journal-title":"Front. Mar. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0410","doi-asserted-by":"crossref","first-page":"514","DOI":"10.1016\/j.bbrc.2006.07.078","article-title":"Aurelin, a novel antimicrobial peptide from jellyfish Aurelia aurita with structural features of defensins and channel-blocking toxins","volume":"348","author":"Ovchinnikova","year":"2006","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0415","doi-asserted-by":"crossref","first-page":"514","DOI":"10.1016\/j.bbrc.2006.07.078","article-title":"Aurelin, a novel antimicrobial peptide from jellyfish Aurelia aurita with structural features of defensins and channel-blocking toxins","volume":"348","author":"Ovchinnikova","year":"2006","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0420","doi-asserted-by":"crossref","first-page":"785","DOI":"10.3390\/ijms17050785","article-title":"Marine antimicrobial peptides: nature provides templates for the Design of Novel Compounds against pathogenic Bacteria","volume":"17","author":"Falanga","year":"2016","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0425","doi-asserted-by":"crossref","DOI":"10.3389\/fmars.2022.1112595","article-title":"Antimicrobial peptides from marine animals: sources, structures, mechanisms and the potential for drug development","volume":"9","author":"Wang","year":"2023","journal-title":"Front. Mar. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0430","series-title":"Phylogeny of Annelida, in: Evolution of Venomous Animals and their Toxins","first-page":"1","author":"Struck","year":"2015"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0435","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1186\/s12929-024-01007-8","article-title":"Promising antibacterial efficacy of arenicin peptides against the emerging opportunistic pathogen mycobacterium abscessus","volume":"31","author":"Casanova","year":"2024","journal-title":"J. Biomed. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0440","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1002\/psc.2843","article-title":"Bioengineering and functional characterization of arenicin shortened analogs with enhanced antibacterial activity and cell selectivity","volume":"22","author":"Panteleev","year":"2016","journal-title":"J. Pept. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0445","article-title":"Demystifying the Capitella capitata complex (Annelida, Capitellidae) diversity by morphological and molecular data along the Brazilian coast","volume":"12","author":"Silva","year":"2017","journal-title":"PLoS One"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0450","doi-asserted-by":"crossref","first-page":"503","DOI":"10.3390\/md21100503","article-title":"Marine invertebrate antimicrobial peptides and their potential as novel peptide antibiotics","volume":"21","author":"Guryanova","year":"2023","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0455","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1186\/s10152-019-0524-z","article-title":"Progress and perspectives in the discovery of polychaete worms (Annelida) of the world","volume":"73","author":"Pamungkas","year":"2019","journal-title":"Helgol. Mar. Res."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0460","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1111\/brv.12439","article-title":"The evolution of molluscs","volume":"94","author":"Wanninger","year":"2019","journal-title":"Biol. Rev."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0465","doi-asserted-by":"crossref","first-page":"2759","DOI":"10.1242\/jcs.113.15.2759","article-title":"Differential distribution and defence involvement of antimicrobial peptides in mussel","volume":"113","author":"Mitta","year":"2000","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0470","doi-asserted-by":"crossref","first-page":"12954","DOI":"10.1074\/jbc.275.17.12954","article-title":"Involvement of Mytilins in mussel antimicrobial defense","volume":"275","author":"Mitta","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0475","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1016\/j.fsi.2020.02.020","article-title":"Myticusin-beta, antimicrobial peptide from the marine bivalve, Mytilus coruscus","volume":"99","author":"Oh","year":"2020","journal-title":"Fish Shellfish Immunol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0480","doi-asserted-by":"crossref","first-page":"261","DOI":"10.3390\/md15080261","article-title":"Myticalins: a novel multigenic family of linear, cationic antimicrobial peptides from marine mussels (Mytilus spp.)","volume":"15","author":"Leoni","year":"2017","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0485","doi-asserted-by":"crossref","first-page":"261","DOI":"10.3390\/md15080261","article-title":"Myticalins: a novel multigenic family of linear, cationic antimicrobial peptides from marine mussels (Mytilus spp.)","volume":"15","author":"Leoni","year":"2017","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0490","doi-asserted-by":"crossref","first-page":"1340","DOI":"10.3390\/molecules25061340","article-title":"Resistance of gram-negative Bacteria to current antibacterial agents and approaches to resolve it","volume":"25","author":"Breijyeh","year":"2020","journal-title":"Molecules"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0495","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0023140","article-title":"Mytilus galloprovincialis Myticin C: a chemotactic molecule with antiviral activity and Immunoregulatory properties","volume":"6","author":"Balseiro","year":"2011","journal-title":"PLoS One"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0500","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1080\/11250003.2014.922128","article-title":"Antimicrobial peptides from echinoderms as antibiofilm agents: a natural strategy to combat bacterial infections","volume":"81","author":"Schillaci","year":"2014","journal-title":"Ital. J. Zool."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0505","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1111\/j.1365-2672.2009.04394.x","article-title":"Antimicrobial and antistaphylococcal biofilm activity from the sea urchin Paracentrotus lividus","volume":"108","author":"Schillaci","year":"2010","journal-title":"J. Appl. Microbiol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0510","doi-asserted-by":"crossref","first-page":"159","DOI":"10.3390\/md17030159","article-title":"A synthetic derivative of antimicrobial peptide Holothuroidin 2 from Mediterranean Sea cucumber (Holothuria tubulosa) in the control of listeria monocytogenes","volume":"17","author":"Cusimano","year":"2019","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0515","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1016\/j.dci.2018.05.002","article-title":"Identification of a novel antimicrobial peptide from the sea star Patiria pectinifera","volume":"86","author":"Kim","year":"2018","journal-title":"Dev. Comp. Immunol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0520","doi-asserted-by":"crossref","first-page":"1430","DOI":"10.1016\/j.dci.2008.06.013","article-title":"Strongylocins, novel antimicrobial peptides from the green sea urchin, Strongylocentrotus droebachiensis","volume":"32","author":"Li","year":"2008","journal-title":"Dev. Comp. Immunol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0525","doi-asserted-by":"crossref","first-page":"959","DOI":"10.1016\/j.dci.2010.04.004","article-title":"Centrocins: isolation and characterization of novel dimeric antimicrobial peptides from the green sea urchin, Strongylocentrotus droebachiensis","volume":"34","author":"Li","year":"2010","journal-title":"Dev. Comp. Immunol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0530","first-page":"183895","article-title":"Tachyplesin and CyLoP-1 as efficient anti-mycobacterial peptides: a novel finding","volume":"2022","author":"Priya","year":"1864","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0535","doi-asserted-by":"crossref","unstructured":"T. Kushibiki, M. Kamiya, T. Aizawa, Y. Kumaki, T. Kikukawa, M. Mizuguchi, M. Demura, S. Kawabata, K. Kawano, Interaction between tachyplesin I, an antimicrobial peptide derived from horseshoe crab, and lipopolysaccharide, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1844 (2014) 527\u2013534. doi:https:\/\/doi.org\/10.1016\/j.bbapap.2013.12.017.","DOI":"10.1016\/j.bbapap.2013.12.017"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0540","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1007\/BF00354079","article-title":"Cardioinhibitory peptides from Limulus polyphemus: modulation of the neurogenic heart","volume":"164","author":"Gaus","year":"1994","journal-title":"J. Comp. Physiol. B."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0545","doi-asserted-by":"crossref","first-page":"1260","DOI":"10.1007\/PL00000764","article-title":"Penaeidins, a family of antimicrobial peptides from penaeid shrimp (Crustacea, Decapoda)","volume":"57","author":"Destoumieux","year":"2000","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0550","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1016\/j.fsi.2019.03.007","article-title":"Molecular characterization, recombinant expression and bioactivity profile of an antimicrobial peptide, Ss-arasin from the Indian mud crab, Scylla serrata","volume":"88","author":"Anju","year":"2019","journal-title":"Fish Shellfish Immunol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0555","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1016\/j.fsi.2019.03.007","article-title":"Molecular characterization, recombinant expression and bioactivity profile of an antimicrobial peptide, Ss-arasin from the Indian mud crab, Scylla serrata","volume":"88","author":"Anju","year":"2019","journal-title":"Fish Shellfish Immunol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0560","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1111\/febs.13178","article-title":"Marine antimicrobial peptide tachyplesin as an efficient nanocarrier for macromolecule delivery in plant and mammalian cells","volume":"282","author":"Jain","year":"2015","journal-title":"FEBS J."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0565","doi-asserted-by":"crossref","first-page":"1460","DOI":"10.1128\/AAC.36.7.1460","article-title":"Mechanisms of antibacterial action of tachyplesins and polyphemusins, a group of antimicrobial peptides isolated from horseshoe crab hemocytes","volume":"36","author":"Ohta","year":"1992","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0570","doi-asserted-by":"crossref","first-page":"1491","DOI":"10.1099\/vir.0.009621-0","article-title":"Role of anti-lipopolysaccharide factor from the black tiger shrimp, Penaeus monodon, in protection from white spot syndrome virus infection","volume":"90","author":"Tharntada","year":"2009","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0575","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/j.peptides.2018.12.004","article-title":"Epinecidin-1: a marine fish antimicrobial peptide with therapeutic potential against trichomonas vaginalis infection in mice","volume":"112","author":"Huang","year":"2019","journal-title":"Peptides (N.Y.)"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0580","doi-asserted-by":"crossref","first-page":"145","DOI":"10.3390\/md20020145","article-title":"Expression of the antimicrobial peptide Piscidin 1 and neuropeptides in fish gill and skin: a potential participation in neuro-immune interaction","volume":"20","author":"Zaccone","year":"2022","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0585","doi-asserted-by":"crossref","first-page":"396","DOI":"10.1016\/j.jsps.2018.01.001","article-title":"Recent updates of marine antimicrobial peptides","volume":"26","author":"Semreen","year":"2018","journal-title":"Saudi Pharm. J."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0590","doi-asserted-by":"crossref","DOI":"10.1016\/j.biopha.2022.113189","article-title":"Cathelicidins and defensins antimicrobial host defense peptides in the treatment of TB and HIV: Pharmacogenomic and nanomedicine approaches towards improved therapeutic outcomes","volume":"151","author":"Dlozi","year":"2022","journal-title":"Biomed. Pharmacother."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0595","doi-asserted-by":"crossref","DOI":"10.1016\/j.biopha.2022.113189","article-title":"Cathelicidins and defensins antimicrobial host defense peptides in the treatment of TB and HIV: Pharmacogenomic and nanomedicine approaches towards improved therapeutic outcomes","volume":"151","author":"Dlozi","year":"2022","journal-title":"Biomed. Pharmacother."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0600","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/S1542-0124(12)70111-8","article-title":"Defensins and other antimicrobial peptides at the ocular surface","volume":"2","author":"McDermott","year":"2004","journal-title":"Ocul. Surf."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0605","doi-asserted-by":"crossref","first-page":"9251","DOI":"10.3390\/ijms24119251","article-title":"Antibacterial activity and mechanisms of TroHepc2-22, a derived peptide of Hepcidin2 from Golden pompano (Trachinotus ovatus)","volume":"24","author":"Zhang","year":"2023","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0610","doi-asserted-by":"crossref","DOI":"10.1016\/j.aquaculture.2023.739430","article-title":"Antimicrobial activity of histone1-derived peptides from large yellow croaker Larimichthys crocea","volume":"570","author":"Ma","year":"2023","journal-title":"Aquaculture"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0615","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1016\/j.nano.2016.07.018","article-title":"Self-assembled cationic amphiphiles as antimicrobial peptides mimics: role of hydrophobicity, linkage type, and assembly state","volume":"13","author":"Zhang","year":"2017","journal-title":"Nanomedicine"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0620","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/j.actbio.2015.02.023","article-title":"Characterization of antimicrobial activity and mechanisms of low amphipathic peptides with different \u03b1-helical propensity","volume":"18","author":"Zhu","year":"2015","journal-title":"Acta Biomater."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0625","doi-asserted-by":"crossref","first-page":"471","DOI":"10.3390\/ph14050471","article-title":"Physicochemical features and peculiarities of interaction of AMP with the membrane","volume":"14","author":"Pirtskhalava","year":"2021","journal-title":"Pharmaceuticals"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0630","doi-asserted-by":"crossref","first-page":"1600","DOI":"10.1016\/j.bbamem.2009.04.012","article-title":"Binding of amphipathic \u03b1-helical antimicrobial peptides to lipid membranes: lessons from temporins B and L","volume":"1788","author":"Mahalka","year":"2009","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0635","doi-asserted-by":"crossref","first-page":"439","DOI":"10.3390\/ph16030439","article-title":"Glycosylation and Lipidation strategies: approaches for improving antimicrobial peptide efficacy","volume":"16","author":"Bellavita","year":"2023","journal-title":"Pharmaceuticals"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0640","doi-asserted-by":"crossref","first-page":"442","DOI":"10.1021\/acsinfecdis.6b00045","article-title":"Contribution of Amphipathicity and hydrophobicity to the antimicrobial activity and cytotoxicity of \u03b2-hairpin peptides","volume":"2","author":"Edwards","year":"2016","journal-title":"ACS Infect. Dis."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0645","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1002\/cbic.201402581","article-title":"Rational Design of Alpha-Helical Antimicrobial Peptides: Do\u2019s and Don\u2019ts","volume":"16","author":"Uggerh\u00f8j","year":"2015","journal-title":"ChemBioChem"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0650","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/0014-5793(88)81405-4","article-title":"A two-dimensional NMR study of the antimicrobial peptide magainin 2","volume":"227","author":"Marion","year":"1988","journal-title":"FEBS Lett."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0655","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1111\/j.0105-2896.2004.0124.x","article-title":"Anti-microbial peptides: from invertebrates to vertebrates","volume":"198","author":"Bulet","year":"2004","journal-title":"Immunol. Rev."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0660","doi-asserted-by":"crossref","first-page":"14543","DOI":"10.1038\/s41598-017-15149-3","article-title":"High-level heterologous production and functional secretion by recombinant Pichia pastoris of the shortest proline-rich antibacterial honeybee peptide Apidaecin","volume":"7","author":"Chen","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0665","doi-asserted-by":"crossref","first-page":"612","DOI":"10.1016\/j.ibmb.2013.03.013","article-title":"Gloverins of the silkworm Bombyx mori: structural and binding properties and activities","volume":"43","author":"Yi","year":"2013","journal-title":"Insect Biochem. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0670","doi-asserted-by":"crossref","first-page":"785","DOI":"10.3390\/ijms17050785","article-title":"Marine antimicrobial peptides: nature provides templates for the Design of Novel Compounds against pathogenic Bacteria","volume":"17","author":"Falanga","year":"2016","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0675","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1146\/annurev-animal-022114-110903","article-title":"Molecular basis for adaptation of oysters to stressful marine intertidal environments","volume":"4","author":"Zhang","year":"2016","journal-title":"Annu. Rev. Anim. Biosci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0680","doi-asserted-by":"crossref","DOI":"10.3389\/fmars.2021.667764","article-title":"Marine organisms as a rich source of biologically active peptides","volume":"8","author":"Macedo","year":"2021","journal-title":"Front. Mar. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0685","doi-asserted-by":"crossref","first-page":"12182","DOI":"10.1021\/ja104524q","article-title":"Genetic interception and structural characterization of Thiopeptide cyclization precursors from Bacillus cereus","volume":"132","author":"Bowers","year":"2010","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0690","doi-asserted-by":"crossref","first-page":"11787","DOI":"10.3390\/ijms241411787","article-title":"Novel antimicrobial peptides from saline environments active against E. Faecalis and S. Aureus: identification, characterisation and potential usage","volume":"24","author":"Lach","year":"2023","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0695","doi-asserted-by":"crossref","first-page":"3491","DOI":"10.1021\/ja411119m","article-title":"High-resolution structures and orientations of antimicrobial peptides Piscidin 1 and Piscidin 3 in fluid bilayers reveal tilting, kinking, and bilayer immersion","volume":"136","author":"Perrin","year":"2014","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0700","doi-asserted-by":"crossref","first-page":"6255","DOI":"10.1021\/bi200746t","article-title":"Molecular mechanism of action of \u03b2-hairpin antimicrobial peptide Arenicin: oligomeric structure in Dodecylphosphocholine micelles and pore formation in planar lipid bilayers","volume":"50","author":"Shenkarev","year":"2011","journal-title":"Biochemistry"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0705","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.1501334112","article-title":"Optimized deep-targeted proteotranscriptomic profiling reveals unexplored Conus toxin diversity and novel cysteine frameworks","volume":"112","author":"Lavergne","year":"2015","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0710","doi-asserted-by":"crossref","first-page":"9692","DOI":"10.3390\/ijms21249692","article-title":"Lipidation of antimicrobial peptides as a design strategy for future alternatives to antibiotics","volume":"21","author":"Rounds","year":"2020","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0715","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1096\/fasebj.14.2.231","article-title":"The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains","volume":"14","author":"Kay","year":"2000","journal-title":"FASEB J."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0720","first-page":"33","article-title":"Epinecidin-1, a highly potent marine antimicrobial peptide with anticancer and immunomodulatory activities, BMC","volume":"20","author":"Neshani","year":"2019","journal-title":"Pharmacol. Toxicol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0725","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1016\/j.actbio.2020.03.024","article-title":"Identification of new dermaseptins with self-assembly tendency: membrane disruption, biofilm eradication, and infected wound healing efficacy","volume":"109","author":"Song","year":"2020","journal-title":"Acta Biomater."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0730","doi-asserted-by":"crossref","first-page":"904","DOI":"10.1039\/C5NP00010F","article-title":"Defensive symbioses of animals with prokaryotic and eukaryotic microorganisms","volume":"32","author":"Fl\u00f3rez","year":"2015","journal-title":"Nat. Prod. Rep."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0735","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1038\/s42003-018-0224-2","article-title":"Structure-function-guided exploration of the antimicrobial peptide polybia-CP identifies activity determinants and generates synthetic therapeutic candidates","volume":"1","author":"Torres","year":"2018","journal-title":"Commun. Biol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0740","first-page":"757","article-title":"Structure\u2013activity relationships of antibacterial peptides, microb","volume":"16","author":"Ciulla","year":"2023","journal-title":"Biotechnol"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0745","doi-asserted-by":"crossref","unstructured":"K.J. Skowron, C. Baliga, T. Johnson, K.M. Kremiller, A. Castroverde, T.T. Dean, A.C. Allen, A.M. Lopez-Hernandez, E. V. Aleksandrova, D. Klepacki, A.S. Mankin, Y.S. Polikanov, T.W. Moore, Structure\u2013Activity Relationships of the Antimicrobial Peptide Natural Product Apidaecin, J. Med. Chem. 66 (2023) 11831\u201311842. doi:https:\/\/doi.org\/10.1021\/acs.jmedchem.3c00406.","DOI":"10.1021\/acs.jmedchem.3c00406"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0750","doi-asserted-by":"crossref","first-page":"1506","DOI":"10.3390\/pharmaceutics15051506","article-title":"Review: structure-activity relationship of antimicrobial Peptoids","volume":"15","author":"Nyembe","year":"2023","journal-title":"Pharmaceutics"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0755","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1007\/s11274-018-2444-5","article-title":"Antimicrobial peptides: biochemical determinants of activity and biophysical techniques of elucidating their functionality","volume":"34","author":"Shagaghi","year":"2018","journal-title":"World J. Microbiol. Biotechnol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0760","doi-asserted-by":"crossref","first-page":"397","DOI":"10.3390\/md20060397","article-title":"Marine cyclic peptides: antimicrobial activity and synthetic strategies","volume":"20","author":"Ribeiro","year":"2022","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0765","doi-asserted-by":"crossref","first-page":"397","DOI":"10.3390\/md20060397","article-title":"Marine cyclic peptides: antimicrobial activity and synthetic strategies","volume":"20","author":"Ribeiro","year":"2022","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0770","doi-asserted-by":"crossref","first-page":"609","DOI":"10.3390\/md21120609","article-title":"Therapeutic potential of marine-derived cyclic peptides as Antiparasitic agents","volume":"21","author":"Ribeiro","year":"2023","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0775","doi-asserted-by":"crossref","unstructured":"E.W. Schmidt, A.Y. Obraztsova, S.K. Davidson, D.J. Faulkner, M.G. Haygood, Identification of the antifungal peptide-containing symbiont of the marine sponge Theonella swinhoei as a novel \u03b4-proteobacterium, \u201c Candidatus Entotheonella palauensis,\u201d Mar. Biol. 136 (2000) 969\u2013977. doi:https:\/\/doi.org\/10.1007\/s002270000273.","DOI":"10.1007\/s002270000273"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0780","doi-asserted-by":"crossref","first-page":"338","DOI":"10.1021\/jm00002a015","article-title":"Halicylindramides A-C, antifungal and cytotoxic depsipeptides from the marine sponge Halichondria cylindrata","volume":"38","author":"Li","year":"1995","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0785","doi-asserted-by":"crossref","first-page":"5319","DOI":"10.1021\/jo800583b","article-title":"Homophymine a, an anti-HIV Cyclodepsipeptide from the sponge Homophymia sp","volume":"73","author":"Zampella","year":"2008","journal-title":"J. Org. Chem."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0790","doi-asserted-by":"crossref","first-page":"3123","DOI":"10.1021\/ja00271a062","article-title":"A modified peptide from a Jaspis sponge, with insecticidal and antifungal activity","volume":"108","author":"Mark","year":"1986","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0795","doi-asserted-by":"crossref","first-page":"4344","DOI":"10.1021\/jo100076g","article-title":"Mutremdamide a and Koshikamides C\u2212H, peptide inhibitors of HIV-1 entry from different Theonella species","volume":"75","author":"Plaza","year":"2010","journal-title":"J. Org. Chem."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0800","doi-asserted-by":"crossref","first-page":"5899","DOI":"10.1021\/ja990582o","article-title":"Papuamides a\u2212D, HIV-inhibitory and cytotoxic Depsipeptides from the sponges Theonella mirabilis and Theonella swinhoei collected in Papua New Guinea","volume":"121","author":"Ford","year":"1999","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0805","doi-asserted-by":"crossref","first-page":"1582","DOI":"10.1021\/np060229d","article-title":"Theopapuamide, a cyclic Depsipeptide from a Papua New Guinea Lithistid sponge Theonella swinhoei","volume":"69","author":"Ratnayake","year":"2006","journal-title":"J. Nat. Prod."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0810","doi-asserted-by":"crossref","first-page":"504","DOI":"10.1021\/jo802232u","article-title":"Celebesides a\u2212C and Theopapuamides B\u2212D, Depsipeptides from an Indonesian sponge that inhibit HIV-1 entry","volume":"74","author":"Plaza","year":"2009","journal-title":"J. Org. Chem."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0815","doi-asserted-by":"crossref","first-page":"397","DOI":"10.3390\/md20060397","article-title":"Marine cyclic peptides: antimicrobial activity and synthetic strategies","volume":"20","author":"Ribeiro","year":"2022","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0820","doi-asserted-by":"crossref","first-page":"7593","DOI":"10.1016\/j.tet.2011.07.053","article-title":"Antimalarial and antituberculosis substances from Streptomyces sp. BCC26924","volume":"67","author":"Intaraudom","year":"2011","journal-title":"Tetrahedron"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0825","doi-asserted-by":"crossref","first-page":"1628","DOI":"10.1039\/C8NP00076J","article-title":"Piperazic acid-containing natural products: structures and biosynthesis","volume":"36","author":"Morgan","year":"2019","journal-title":"Nat. Prod. Rep."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0830","doi-asserted-by":"crossref","DOI":"10.1002\/pep2.24122","article-title":"Antimicrobial peptides under clinical investigation","volume":"111","author":"Koo","year":"2019","journal-title":"Pept. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0835","doi-asserted-by":"crossref","first-page":"76","DOI":"10.3390\/md14040076","article-title":"Potential pharmacological resources: natural bioactive compounds from marine-derived Fungi","volume":"14","author":"Jin","year":"2016","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0840","first-page":"119","article-title":"The origin of cephalosporins","volume":"37","author":"Nakajima","year":"2003","journal-title":"Yakushigaku Zasshi"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0845","doi-asserted-by":"crossref","unstructured":"T. OHYAMA, Y. KURIHARA, Y. ONO, T. ISHIKAWA, S. MIYAKOSHI, K. HAMANO, M. ARAEI, T. SUZUKI, H. IGARI, Y. SUZUKI, M. INUKAI, Arborcandins A, B, C, D, E and F, Novel 1,3-.BETA.-glucan synthase inhibitors. Production and biological activity., J. Antibiot. (Tokyo) 53 (2000) 1108\u20131116. doi:https:\/\/doi.org\/10.7164\/antibiotics.53.1108.","DOI":"10.7164\/antibiotics.53.1108"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0850","doi-asserted-by":"crossref","unstructured":"K. TAKESAKO, K. IKAI, F. HARUNA, M. ENDO, K. SHIMANAKA, E. SONO, T. NAKAMURA, I. KATO, H. YAMAGUCHI, Aureobasidins, new antifungal antibiotics. Taxonomy, fermentation, isolation, and properties., J Antibiot (Tokyo) 44 (1991) 919\u2013924. doi:https:\/\/doi.org\/10.7164\/antibiotics.44.919.","DOI":"10.7164\/antibiotics.44.919"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0855","doi-asserted-by":"crossref","first-page":"1361","DOI":"10.1016\/j.bmc.2008.12.009","article-title":"Isolation, structure and biological activity of phomafungin, a cyclic lipodepsipeptide from a widespread tropical Phoma sp","volume":"17","author":"Herath","year":"2009","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0860","doi-asserted-by":"crossref","first-page":"397","DOI":"10.3390\/md20060397","article-title":"Marine cyclic peptides: antimicrobial activity and synthetic strategies","volume":"20","author":"Ribeiro","year":"2022","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0865","doi-asserted-by":"crossref","first-page":"1910","DOI":"10.1021\/acs.jnatprod.5b00266","article-title":"Callyaerins from the marine sponge Callyspongia aerizusa: cyclic peptides with Antitubercular activity","volume":"78","author":"Daletos","year":"2015","journal-title":"J. Nat. Prod."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0870","first-page":"1755","article-title":"The anti-tubercular callyaerins target the mycobacterium tuberculosis-specific non-essential membrane protein Rv2113, cell","volume":"31","author":"Podlesainski","year":"2024","journal-title":"Chem. Biol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0875","doi-asserted-by":"crossref","first-page":"504","DOI":"10.1021\/jo802232u","article-title":"Celebesides A-C and theopapuamides B-D, depsipeptides from an Indonesian sponge that inhibit HIV-1 entry","volume":"74","author":"Plaza","year":"2009","journal-title":"J. Org. Chem."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0880","doi-asserted-by":"crossref","first-page":"118","DOI":"10.62347\/TUVQ7468","article-title":"Marine bioactive peptides with anticancer potential, a narrative review","volume":"15","author":"Rafieezadeh","year":"2024","journal-title":"Int J Biochem Mol Biol"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0885","doi-asserted-by":"crossref","first-page":"14539","DOI":"10.1038\/s41598-021-93285-7","article-title":"Isolation, characterization, anti-MRSA evaluation, and in-silico multi-target anti-microbial validations of actinomycin X2 and actinomycin D produced by novel Streptomyces smyrnaeus UKAQ_23","volume":"11","author":"Qureshi","year":"2021","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0890","doi-asserted-by":"crossref","first-page":"4788","DOI":"10.1021\/acs.jafc.3c08600","article-title":"Antibacterial mechanism, control efficiency, and nontarget toxicity evaluation of Actinomycin X2 against Xanthomonas citri Subsp. citri","volume":"72","author":"Gao","year":"2024","journal-title":"J. Agric. Food Chem."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0895","doi-asserted-by":"crossref","first-page":"1164","DOI":"10.1021\/np4011037","article-title":"Cyclohexadepsipeptides of the Isaridin class from the marine-derived fungus Beauveria felina EN-135","volume":"77","author":"Du","year":"2014","journal-title":"J. Nat. Prod."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0900","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1016\/j.cis.2017.06.001","article-title":"The interaction of antimicrobial peptides with membranes","volume":"247","author":"Travkova","year":"2017","journal-title":"Adv. Colloid Interf. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0905","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.tifs.2021.01.005","article-title":"The structure-mechanism relationship and mode of actions of antimicrobial peptides: a review","volume":"109","author":"Li","year":"2021","journal-title":"Trends Food Sci. Technol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0910","doi-asserted-by":"crossref","first-page":"7546","DOI":"10.3390\/molecules27217546","article-title":"Marine antimicrobial peptides-based strategies for tackling bacterial biofilm and biofouling challenges","volume":"27","author":"Patra","year":"2022","journal-title":"Molecules"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0915","doi-asserted-by":"crossref","DOI":"10.3389\/fmedt.2021.640981","article-title":"Developing antimicrobial synergy with AMPs","volume":"3","author":"Duong","year":"2021","journal-title":"Front Med. Technol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0920","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2023.115377","article-title":"Antimicrobial peptides: structure, mechanism, and modification","volume":"255","author":"Chen","year":"2023","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0925","doi-asserted-by":"crossref","first-page":"143","DOI":"10.3109\/07388551.2011.594423","article-title":"Antimicrobial peptides: key components of the innate immune system","volume":"32","author":"Pasupuleti","year":"2012","journal-title":"Crit. Rev. Biotechnol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0930","doi-asserted-by":"crossref","first-page":"763","DOI":"10.3390\/md20120763","article-title":"Polypharmacological cell-penetrating peptides from venomous marine animals based on Immunomodulating, antimicrobial, and anticancer properties","volume":"20","author":"Hemmati","year":"2022","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0935","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1111\/exd.12929","article-title":"Antimicrobial peptides and wound healing: biological and therapeutic considerations","volume":"25","author":"Mangoni","year":"2016","journal-title":"Exp. Dermatol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0940","doi-asserted-by":"crossref","first-page":"763","DOI":"10.3390\/md20120763","article-title":"Polypharmacological cell-penetrating peptides from venomous marine animals based on Immunomodulating, antimicrobial, and anticancer properties","volume":"20","author":"Hemmati","year":"2022","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0945","doi-asserted-by":"crossref","DOI":"10.1016\/j.cej.2023.145923","article-title":"Enhancing the stability of antimicrobial peptides: from design strategies to applications","volume":"475","author":"Xu","year":"2023","journal-title":"Chem. Eng. J."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0950","doi-asserted-by":"crossref","first-page":"975","DOI":"10.1039\/D1GC04387K","article-title":"Sustainability in peptide chemistry: current synthesis and purification technologies and future challenges","volume":"24","author":"Ferrazzano","year":"2022","journal-title":"Green Chem."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0955","doi-asserted-by":"crossref","first-page":"1073","DOI":"10.3390\/polym13071073","article-title":"Polymeric materials used for immobilisation of Bacteria for the bioremediation of contaminants in water","volume":"13","author":"Berillo","year":"2021","journal-title":"Polymers (Basel)"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0960","doi-asserted-by":"crossref","first-page":"24250","DOI":"10.1039\/D3RA04100J","article-title":"A novel series of dipeptide derivatives containing indole-3-carboxylic acid conjugates as potential antimicrobial agents: the design, solid phase peptide synthesis, in vitro biological evaluation, and molecular docking study","volume":"13","author":"Tivari","year":"2023","journal-title":"RSC Adv."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0965","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/j.ejmech.2019.02.024","article-title":"Microwave-assisted solid-phase synthesis of antisense acpP peptide nucleic acid-peptide conjugates active against colistin- and tigecycline-resistant E. Coli and K. Pneumoniae","volume":"168","author":"Hansen","year":"2019","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0970","doi-asserted-by":"crossref","first-page":"6014","DOI":"10.1021\/ol2024696","article-title":"Amino acid building blocks for efficient Fmoc solid-phase synthesis of peptides Adenylylated at serine or threonine","volume":"13","author":"Albers","year":"2011","journal-title":"Org. Lett."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0975","doi-asserted-by":"crossref","first-page":"439","DOI":"10.3390\/ph16030439","article-title":"Glycosylation and Lipidation strategies: approaches for improving antimicrobial peptide efficacy","volume":"16","author":"Bellavita","year":"2023","journal-title":"Pharmaceuticals"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0980","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2023.115680","article-title":"Conjugation of antimicrobial peptides to enhance therapeutic efficacy","volume":"259","author":"Selvaraj","year":"2023","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0985","doi-asserted-by":"crossref","first-page":"471","DOI":"10.3390\/ph14050471","article-title":"Physicochemical features and peculiarities of interaction of AMP with the membrane","volume":"14","author":"Pirtskhalava","year":"2021","journal-title":"Pharmaceuticals"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0990","doi-asserted-by":"crossref","first-page":"771","DOI":"10.1080\/17460441.2016.1201058","article-title":"Progress with peptide scanning to study structure-activity relationships: the implications for drug discovery","volume":"11","author":"Eustache","year":"2016","journal-title":"Expert Opin. Drug Discov."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb0995","doi-asserted-by":"crossref","first-page":"2383","DOI":"10.3390\/ijms20102383","article-title":"A comprehensive Review on current advances in peptide drug development and design","volume":"20","author":"Lee","year":"2019","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1000","doi-asserted-by":"crossref","first-page":"975","DOI":"10.1039\/D1GC04387K","article-title":"Sustainability in peptide chemistry: current synthesis and purification technologies and future challenges","volume":"24","author":"Ferrazzano","year":"2022","journal-title":"Green Chem."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1005","doi-asserted-by":"crossref","DOI":"10.1016\/j.biotechadv.2022.107962","article-title":"Strategies employed in the design of antimicrobial peptides with enhanced proteolytic stability","volume":"59","author":"Lai","year":"2022","journal-title":"Biotechnol. Adv."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1010","doi-asserted-by":"crossref","first-page":"674","DOI":"10.3390\/pharmaceutics16050674","article-title":"Novel drug delivery systems: An important direction for drug innovation Research and Development","volume":"16","author":"Chen","year":"2024","journal-title":"Pharmaceutics"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1015","doi-asserted-by":"crossref","first-page":"2113","DOI":"10.3390\/pharmaceutics15082113","article-title":"An overview of stimuli-responsive intelligent antibacterial nanomaterials","volume":"15","author":"Zhang","year":"2023","journal-title":"Pharmaceutics"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1020","first-page":"9","article-title":"Progress and future of the computational design of antimicrobial peptides (AMPs): bio-inspired functional molecules, digital","volume":"3","author":"Nedyalkova","year":"2024","journal-title":"Discovery"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1025","doi-asserted-by":"crossref","first-page":"363","DOI":"10.3390\/md20060363","article-title":"The immune system of marine organisms as source for drugs against infectious diseases","volume":"20","author":"Falco","year":"2022","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1030","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijpharm.2023.122918","article-title":"Multilayered nanofibrous scaffold of polyvinyl alcohol\/gelatin\/poly (lactic-co-glycolic acid) enriched with hemostatic\/antibacterial agents for rapid acute hemostatic wound healing","volume":"638","author":"Pandey","year":"2023","journal-title":"Int. J. Pharm."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1035","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/S0924-8579(00)00131-X","article-title":"Interaction between antibiotics and non-conventional antibiotics on bacteria","volume":"14","author":"Gunics","year":"2000","journal-title":"Int. J. Antimicrob. Agents"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1040","doi-asserted-by":"crossref","first-page":"5397","DOI":"10.2147\/IJN.S464046","article-title":"Resveratrol-ampicillin dual-drug loaded Polyvinylpyrrolidone\/polyvinyl alcohol biomimic electrospun nanofiber enriched with collagen for efficient burn wound repair","volume":"19","author":"Kanaujiya","year":"2024","journal-title":"Int. J. Nanomedicine"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1045","doi-asserted-by":"crossref","DOI":"10.1021\/acs.jmedchem.4c02039","article-title":"Improving the stability and anti-infective activity of sea turtle AMPs using multiple structural modification strategies","author":"Ye","year":"2024","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1050","doi-asserted-by":"crossref","first-page":"291","DOI":"10.3390\/pharmaceutics15010291","article-title":"Combined use of antimicrobial peptides with antiseptics against multidrug-resistant Bacteria: pros and cons","volume":"15","author":"Zharkova","year":"2023","journal-title":"Pharmaceutics"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1055","doi-asserted-by":"crossref","first-page":"1840006","DOI":"10.1142\/S0219720018400061","article-title":"Discovery of novel antimicrobial peptides: a transcriptomic study of the sea anemone Cnidopus japonicus","volume":"16","author":"Grafskaia","year":"2018","journal-title":"J. Bioinforma. Comput. Biol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1060","doi-asserted-by":"crossref","first-page":"855","DOI":"10.3390\/antibiotics12050855","article-title":"Teleost Piscidins\u2014in silico perspective of natural peptide antibiotics from marine sources","volume":"12","author":"Asensio-Calavia","year":"2023","journal-title":"Antibiotics"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1065","doi-asserted-by":"crossref","DOI":"10.1016\/j.actatropica.2023.107116","article-title":"Exploring microalgal and cyanobacterial metabolites with antiprotozoal activity against Leishmania and Trypanosoma parasites","volume":"251","author":"Matos","year":"2024","journal-title":"Acta Trop."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1070","doi-asserted-by":"crossref","DOI":"10.3389\/fmicb.2021.785085","article-title":"Marine Invertebrate Peptides: Antimicrobial Peptides","volume":"12","author":"Wu","year":"2021","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1075","doi-asserted-by":"crossref","DOI":"10.3389\/fmars.2022.1112595","article-title":"Antimicrobial peptides from marine animals: sources, structures, mechanisms and the potential for drug development","volume":"9","author":"Wang","year":"2023","journal-title":"Front. Mar. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1080","doi-asserted-by":"crossref","first-page":"503","DOI":"10.3390\/md21100503","article-title":"Marine invertebrate antimicrobial peptides and their potential as novel peptide antibiotics","volume":"21","author":"Guryanova","year":"2023","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1085","doi-asserted-by":"crossref","first-page":"4877","DOI":"10.1016\/j.bmcl.2012.05.071","article-title":"Neamphamide B, new cyclic depsipeptide, as an anti-dormant mycobacterial substance from a Japanese marine sponge of Neamphius sp","volume":"22","author":"Yamano","year":"2012","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1090","doi-asserted-by":"crossref","first-page":"1911","DOI":"10.3390\/md12041911","article-title":"Theonellamide G, a potent antifungal and cytotoxic bicyclic Glycopeptide from the Red Sea marine sponge Theonella swinhoei","volume":"12","author":"Youssef","year":"2014","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1095","doi-asserted-by":"crossref","first-page":"3697","DOI":"10.1128\/AAC.48.10.3697-3701.2004","article-title":"Antimicrobial evaluation of Nocathiacins, a Thiazole peptide class of antibiotics","volume":"48","author":"Pucci","year":"2004","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1100","doi-asserted-by":"crossref","unstructured":"W. LI, J.E. LEET, H.A. AX, D.R. GUSTAVSON, D.M. BROWN, L. TURNER, K. BROWN, J. CLARK, H. YANG, J. FUNG-TOMC, K.S. LAM, Nocathiacins, New Thiazolyl peptide antibiotics from Nocardia sp. I. Taxonomy, fermentation and biological activities., J. Antibiot. (Tokyo) 56 (2003) 226\u2013231. doi:https:\/\/doi.org\/10.7164\/antibiotics.56.226.","DOI":"10.7164\/antibiotics.56.226"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1105","doi-asserted-by":"crossref","first-page":"977","DOI":"10.1021\/ol005630k","article-title":"Synthesis and antifungal activity of Rhodopeptin analogues. 2. Modification of the west amino acid moiety","volume":"2","author":"Nakayama","year":"2000","journal-title":"Org. Lett."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1110","doi-asserted-by":"crossref","unstructured":"R. Montaser, V.J. Paul, H. Luesch, Pitipeptolides C\u2013F, antimycobacterial cyclodepsipeptides from the marine cyanobacterium Lyngbya majuscula from Guam, Phytochemistry 72 (2011) 2068\u20132074. doi:https:\/\/doi.org\/10.1016\/j.phytochem.2011.07.014.","DOI":"10.1016\/j.phytochem.2011.07.014"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1115","first-page":"304","article-title":"Pitipeptolides a and B","volume":"64","author":"Luesch","year":"2001","journal-title":"New Cyclodepsipeptides from the Marine Cyanobacterium Lyngbya majuscula, J Nat Prod"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1120","first-page":"446","article-title":"Recent developments on the synthesis and bioactivity of Ilamycins\/Rufomycins and Cyclomarins","volume":"19","author":"Kazmaier","year":"2021","journal-title":"Marine Cyclopeptides That Demonstrate Anti-Malaria and Anti-Tuberculosis Activity, Mar Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1125","doi-asserted-by":"crossref","first-page":"990","DOI":"10.1016\/j.bbrc.2007.10.110","article-title":"Inhibition of fungal ABC transporters by unnarmicin a and unnarmicin C, novel cyclic peptides from marine bacterium","volume":"364","author":"Tanabe","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1130","doi-asserted-by":"crossref","first-page":"154","DOI":"10.3390\/toxins9050154","article-title":"New disulfide-stabilized fold Provides Sea Anemone peptide to exhibit both antimicrobial and TRPA1 potentiating properties","volume":"9","author":"Logashina","year":"2017","journal-title":"Toxins (Basel)"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1135","article-title":"Characterization and antimicrobial properties from the sea-anemones (Heteractics magnifica and Stichodactyla merten sii) toxins","volume":"3 (4):109\u2013117","author":"Ghosh S","year":"2011","journal-title":"Arch. Appl. Sci. Res."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1140","doi-asserted-by":"crossref","first-page":"3320","DOI":"10.1111\/febs.14194","article-title":"Defensin-neurotoxin dyad in a basally branching metazoan sea anemone","volume":"284","author":"Kim","year":"2017","journal-title":"FEBS J."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1145","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1186\/1476-0711-11-15","article-title":"Analgesic and antibutyrylcholinestrasic activities of the venom prepared from the Mediterranean jellyfish Pelagia noctiluca (Forsskal, 1775)","volume":"11","author":"Ayed","year":"2012","journal-title":"Ann. Clin. Microbiol. Antimicrob."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1150","doi-asserted-by":"crossref","DOI":"10.1155\/2017\/2752716","article-title":"Anticancer effect of Nemopilema nomurai jellyfish venom on HepG2 cells and a tumor xenograft animal model","volume":"2017","author":"Lee","year":"2017","journal-title":"Evid. Based Complement. Alternat. Med."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1155","doi-asserted-by":"crossref","first-page":"771","DOI":"10.1080\/17460441.2016.1201058","article-title":"Progress with peptide scanning to study structure-activity relationships: the implications for drug discovery","volume":"11","author":"Eustache","year":"2016","journal-title":"Expert Opin. Drug Discov."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1160","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1016\/j.actbio.2020.03.024","article-title":"Identification of new dermaseptins with self-assembly tendency: membrane disruption, biofilm eradication, and infected wound healing efficacy","volume":"109","author":"Song","year":"2020","journal-title":"Acta Biomater."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1165","doi-asserted-by":"crossref","first-page":"1839","DOI":"10.1021\/acsinfecdis.2c00080","article-title":"Tachyplesin I analogue peptide as an effective antimicrobial agent against Candida albicans \u2013 Staphylococcus aureus poly-biofilm formation and mixed infection","volume":"8","author":"Miao","year":"2022","journal-title":"ACS Infect. Dis."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1170","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.molimm.2021.08.010","article-title":"Molecular characterisation and biological activity of an antiparasitic peptide from Sciaenops ocellatus and its immune response to Cryptocaryon irritans","volume":"141","author":"Jin","year":"2022","journal-title":"Mol. Immunol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1175","doi-asserted-by":"crossref","first-page":"844","DOI":"10.1007\/s00436-002-0666-8","article-title":"Effect of jasplakinolide on the growth, invasion, and actin cytoskeleton of plasmodium falciparum","volume":"88","author":"Mizuno","year":"2002","journal-title":"Parasitol. Res."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1180","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1002280","article-title":"Evolutionarily divergent, unstable filamentous actin is essential for gliding motility in apicomplexan parasites","volume":"7","author":"Skillman","year":"2011","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1185","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1645\/0022-3395(2001)087[0399:EOJOTG]2.0.CO;2","article-title":"Effect of jasplakinolide on the growth, encystation, and actin cytoskeleton of Entamoeba histolytica and Entamoeba invadens","volume":"87","author":"Makioka","year":"2001","journal-title":"J. Parasitol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1190","doi-asserted-by":"crossref","first-page":"S145","DOI":"10.1016\/S0188-4409(00)00225-3","article-title":"Growth inhibition and actin aggregate formation of Entamoeba histolytica by Jasplakinolide","volume":"31","author":"Makioka","year":"2000","journal-title":"Arch. Med. Res."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1195","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1021\/np0605790","article-title":"Venturamides a and B: antimalarial constituents of the Panamanian marine cyanobacterium Oscillatoria sp","volume":"70","author":"Linington","year":"2007","journal-title":"J. Nat. Prod."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1200","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1021\/np070280x","article-title":"Symplocamide a, a potent Cytotoxin and chymotrypsin inhibitor from the marine cyanobacterium Symploca sp","volume":"71","author":"Linington","year":"2008","journal-title":"J. Nat. Prod."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1205","doi-asserted-by":"crossref","first-page":"1608","DOI":"10.1021\/mp100035f","article-title":"The Antitumoral Depsipeptide IB-01212 kills Leishmania through an apoptosis-like process involving intracellular targets","volume":"7","author":"Luque-Ortega","year":"2010","journal-title":"Mol. Pharm."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1210","doi-asserted-by":"crossref","unstructured":"H. Ogawa, A. Iwasaki, S. Sumimoto, Y. Kanamori, O. Ohno, M. Iwatsuki, A. Ishiyama, R. Hokari, K. Otoguro, S. O\u0305mura, K. Suenaga, Janadolide, a Cyclic Polyketide\u2013Peptide Hybrid Possessing a tert-Butyl Group from an Okeania sp. Marine Cyanobacterium, J. Nat. Prod. 79 (2016) 1862\u20131866. doi:https:\/\/doi.org\/10.1021\/acs.jnatprod.6b00171.","DOI":"10.1021\/acs.jnatprod.6b00171"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1215","doi-asserted-by":"crossref","first-page":"1360","DOI":"10.1016\/j.tetlet.2018.02.034","article-title":"Total synthesis of janadolide","volume":"59","author":"Ojima","year":"2018","journal-title":"Tetrahedron Lett."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1220","doi-asserted-by":"crossref","first-page":"2383","DOI":"10.1021\/acsomega.7b01920","article-title":"Efforts to access the potent Antitrypanosomal marine natural product Janadolide: synthesis of des-tert-butyl Janadolide and its biological evaluation","volume":"3","author":"Athawale","year":"2018","journal-title":"ACS Omega"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1225","doi-asserted-by":"crossref","first-page":"1649","DOI":"10.1021\/acs.jnatprod.1c00234","article-title":"Motobamide, an Antitrypanosomal cyclic peptide from a Leptolyngbya sp","volume":"84","author":"Takahashi","year":"2021","journal-title":"Marine Cyanobacterium, J. Nat. Prod."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1230","doi-asserted-by":"crossref","first-page":"503","DOI":"10.3390\/md21100503","article-title":"Marine invertebrate antimicrobial peptides and their potential as novel peptide antibiotics","volume":"21","author":"Guryanova","year":"2023","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1235","doi-asserted-by":"crossref","DOI":"10.3389\/fmars.2022.1112595","article-title":"Antimicrobial peptides from marine animals: sources, structures, mechanisms and the potential for drug development","volume":"9","author":"Wang","year":"2023","journal-title":"Front. Mar. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1240","doi-asserted-by":"crossref","DOI":"10.3389\/fmars.2022.1112595","article-title":"Antimicrobial peptides from marine animals: sources, structures, mechanisms and the potential for drug development","volume":"9","author":"Wang","year":"2023","journal-title":"Front. Mar. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1245","doi-asserted-by":"crossref","first-page":"3152","DOI":"10.3390\/ijms23063152","article-title":"Bee venom and its major component Melittin attenuated Cutibacterium acnes- and IGF-1-induced acne vulgaris via inactivation of Akt\/mTOR\/SREBP signaling pathway","volume":"23","author":"Gu","year":"2022","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1250","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1111\/cbdd.12020","article-title":"New Alloferon analogues: synthesis and antiviral properties","volume":"81","author":"Kuczer","year":"2013","journal-title":"Chem. Biol. Drug Des."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1255","doi-asserted-by":"crossref","DOI":"10.1016\/j.pestbp.2019.09.012","article-title":"Inhibitory effect of protein Y3 from Coprinus comatus on tobacco mosaic virus","volume":"168","author":"Xiao","year":"2020","journal-title":"Pestic. Biochem. Physiol."},{"issue":"2010","key":"10.1016\/j.ijbiomac.2025.142158_bb1260","first-page":"1168","article-title":"Plectasin, a fungal Defensin, targets the bacterial Cell Wall precursor lipid II","volume":"328","author":"Schneider","year":"1979","journal-title":"Science"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1265","doi-asserted-by":"crossref","first-page":"3446","DOI":"10.1038\/s41598-022-07341-x","article-title":"Gramicidin S and melittin: potential anti-viral therapeutic peptides to treat SARS-CoV-2 infection","volume":"12","author":"Enayathullah","year":"2022","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1270","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1007\/s42485-021-00072-z","article-title":"In silico molecular docking of SARS-CoV-2 surface proteins with microbial non-ribosomal peptides: identification of potential drugs","volume":"12","author":"Bansal","year":"2021","journal-title":"J. Proteins Proteom."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1275","doi-asserted-by":"crossref","DOI":"10.3389\/fchem.2018.00244","article-title":"Comparative pharmacokinetics and preliminary pharmacodynamics evaluation of Piscidin 1 against PRV and PEDV in rats","volume":"6","author":"Lei","year":"2018","journal-title":"Front. Chem."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1280","doi-asserted-by":"crossref","unstructured":"H.B. Hu, T. Huang, H.T. Lu, Jingle Pocket Pharmacy: Building O2O Micro-ecology of Targeted Medicine Delivery, in: Digital Enablement and Innovation in China, WORLD SCIENTIFIC, 2019: pp. 95\u2013101. doi:https:\/\/doi.org\/10.1142\/9789813276369_0014.","DOI":"10.1142\/9789813276369_0014"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1285","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/j.fsi.2014.10.040","article-title":"Transcriptome analysis of medaka following epinecidin-1 and TH1-5 treatment of NNV infection","volume":"42","author":"Wang","year":"2015","journal-title":"Fish Shellfish Immunol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1290","doi-asserted-by":"crossref","unstructured":"H.-N. Huang, C.-Y. Pan, J.-Y. Chen, Grouper (Epinephelus coioides) antimicrobial peptide epinecidin-1 exhibits antiviral activity against foot-and-mouth disease virus in vitro, Peptides (N.Y.) 106 (2018) 91\u201395. doi:https:\/\/doi.org\/10.1016\/j.peptides.2018.07.003.","DOI":"10.1016\/j.peptides.2018.07.003"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1295","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/j.bbrc.2022.08.094","article-title":"Role of interfacial hydrophobicity in antimicrobial peptide magainin 2-induced nanopore formation","volume":"630","author":"Hasan","year":"2022","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1300","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/j.bbrc.2022.08.094","article-title":"Role of interfacial hydrophobicity in antimicrobial peptide magainin 2-induced nanopore formation","volume":"630","author":"Hasan","year":"2022","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1305","doi-asserted-by":"crossref","first-page":"1966","DOI":"10.1016\/j.peptides.2010.07.028","article-title":"A carpet-based mechanism for direct antimicrobial peptide activity against vaccinia virus membranes","volume":"31","author":"Dean","year":"2010","journal-title":"Peptides (N.Y.)"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1310","doi-asserted-by":"crossref","DOI":"10.1016\/j.virusres.2022.198769","article-title":"Anurans against SARS-CoV-2: a review of the potential antiviral action of anurans cutaneous peptides","volume":"315","author":"de Amaral","year":"2022","journal-title":"Virus Res."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1315","doi-asserted-by":"crossref","unstructured":"H.B. Hu, T. Huang, H.T. Lu, Jingle Pocket Pharmacy: Building O2O Micro-ecology of Targeted Medicine Delivery, in: Digital Enablement and Innovation in China, WORLD SCIENTIFIC, 2019: pp. 95\u2013101. doi:https:\/\/doi.org\/10.1142\/9789813276369_0014.","DOI":"10.1142\/9789813276369_0014"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1320","doi-asserted-by":"crossref","first-page":"1343","DOI":"10.1128\/AAC.01448-09","article-title":"Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database","volume":"54","author":"Wang","year":"2010","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1325","doi-asserted-by":"crossref","first-page":"790","DOI":"10.3390\/biom10050790","article-title":"Biological properties of a novel multifunctional host defense peptide from the skin secretion of the Chaco tree frog, Boana raniceps","volume":"10","author":"Santana","year":"2020","journal-title":"Biomolecules"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1330","doi-asserted-by":"crossref","first-page":"7194","DOI":"10.3390\/ijms23137194","article-title":"The inhibition of DNA viruses by the amphibian antimicrobial peptide Temporin G: a Virological study addressing HSV-1 and JPCyV","volume":"23","author":"Marcocci","year":"2022","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1335","first-page":"1","article-title":"Temporin G, an amphibian antimicrobial peptide against influenza and parainfluenza respiratory viruses","volume":"35","author":"De Angelis","year":"2024","journal-title":"Insights into biological activity and mechanism of action, FASEB JOURNAL"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1340","doi-asserted-by":"crossref","DOI":"10.1128\/AAC.02367-17","article-title":"The amphibian antimicrobial peptide Temporin B inhibits in vitro herpes simplex virus 1 infection","volume":"62","author":"Marcocci","year":"2018","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1345","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1021\/np0002379","article-title":"Microspinosamide, a new HIV-inhibitory cyclic Depsipeptide from the marine sponge Sidonops microspinosa","volume":"64","author":"Rashid","year":"2001","journal-title":"J. Nat. Prod."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1350","doi-asserted-by":"crossref","unstructured":"A. Plaza, E. Gustchina, H.L. Baker, M. Kelly, C.A. Bewley, Mirabamides A\u2013D, Depsipeptides from the Sponge Siliquariaspongia mirabilis That Inhibit HIV-1 Fusion, J. Nat. Prod. 70 (2007) 1753\u20131760. doi:https:\/\/doi.org\/10.1021\/np070306k.","DOI":"10.1021\/np070306k"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1355","doi-asserted-by":"crossref","first-page":"1407","DOI":"10.1021\/np040003f","article-title":"Neamphamide a, a new HIV-inhibitory Depsipeptide from the Papua New Guinea marine sponge Neamphius huxleyi","volume":"67","author":"Oku","year":"2004","journal-title":"J. Nat. Prod."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1360","doi-asserted-by":"crossref","first-page":"301","DOI":"10.3390\/md20050301","article-title":"Preclinical development of Seriniquinones as selective Dermcidin modulators for the treatment of melanoma","volume":"20","author":"Hirata","year":"2022","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1365","doi-asserted-by":"crossref","first-page":"40329","DOI":"10.18632\/oncotarget.9612","article-title":"Targeting FOSB with a cationic antimicrobial peptide, TP4, for treatment of triple-negative breast cancer","volume":"7","author":"Ting","year":"2016","journal-title":"Oncotarget"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1370","doi-asserted-by":"crossref","unstructured":"D. KGK, S. Kumari, S. G, R.R. Malla, Marine natural compound cyclo(L-leucyl-L-prolyl) peptide inhibits migration of triple negative breast cancer cells by disrupting interaction of CD151 and EGFR signaling, Chem. Biol. Interact. 315 (2020) 108872. doi:https:\/\/doi.org\/10.1016\/j.cbi.2019.108872.","DOI":"10.1016\/j.cbi.2019.108872"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1375","doi-asserted-by":"crossref","first-page":"7482","DOI":"10.1039\/D2SC02024F","article-title":"Gramicidin a accumulates in mitochondria, reduces ATP levels, induces mitophagy, and inhibits cancer cell growth","volume":"13","author":"Xue","year":"2022","journal-title":"Chem. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1380","first-page":"53","article-title":"Gramicidin inhibits cholangiocarcinoma cell growth by suppressing EGR4, Artif cells Nanomed","volume":"48","author":"Gong","year":"2020","journal-title":"Biotechnol"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1385","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1186\/s40659-019-0264-1","article-title":"Gramicidin inhibits human gastric cancer cell proliferation, cell cycle and induced apoptosis","volume":"52","author":"Chen","year":"2019","journal-title":"Biol. Res."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1390","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1186\/s12935-019-0862-6","article-title":"The ionophore antibiotic gramicidin a inhibits pancreatic cancer stem cells associated with CD47 down-regulation","volume":"19","author":"Wang","year":"2019","journal-title":"Cancer Cell Int."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1395","doi-asserted-by":"crossref","first-page":"929","DOI":"10.3390\/molecules24050929","article-title":"Bee venom and its peptide component Melittin suppress growth and migration of melanoma cells via inhibition of PI3K\/AKT\/mTOR and MAPK pathways","volume":"24","author":"Lim","year":"2019","journal-title":"Molecules"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1400","doi-asserted-by":"crossref","first-page":"5045","DOI":"10.1038\/s41598-020-61876-5","article-title":"Piscidin-1 induces apoptosis via mitochondrial reactive oxygen species-regulated mitochondrial dysfunction in human osteosarcoma cells","volume":"10","author":"Cheng","year":"2020","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1405","article-title":"Navigating the brain: harnessing endogenous cellular hitchhiking for targeting neoplastic and Neuroinflammatory diseases, Asian","author":"Wagh","year":"2025","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1410","doi-asserted-by":"crossref","DOI":"10.1016\/j.brainres.2024.149411","article-title":"Nanoparticle-enhanced delivery of resveratrol for targeted therapy of glioblastoma: modulating the Akt\/GSK-3\u03b2\/NF-kB pathway in C6 glioma cells","volume":"1848","author":"Singh","year":"2025","journal-title":"Brain Res."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1415","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s11010-019-03643-3","article-title":"Pharmacological inhibition of p38 potentiates antimicrobial peptide TP4-induced cell death in glioblastoma cells","volume":"464","author":"Su","year":"2020","journal-title":"Mol. Cell. Biochem."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1420","doi-asserted-by":"crossref","unstructured":"D. KGK, S. Kumari, S. G, R.R. Malla, Marine natural compound cyclo(L-leucyl-L-prolyl) peptide inhibits migration of triple negative breast cancer cells by disrupting interaction of CD151 and EGFR signaling, Chem. Biol. Interact. 315 (2020) 108872. doi:https:\/\/doi.org\/10.1016\/j.cbi.2019.108872.","DOI":"10.1016\/j.cbi.2019.108872"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1425","doi-asserted-by":"crossref","first-page":"1973","DOI":"10.1016\/S0968-0896(02)00014-7","article-title":"New apratoxins of marine cyanobacterial origin from Guam and Palau","volume":"10","author":"Luesch","year":"2002","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1430","doi-asserted-by":"crossref","first-page":"1099","DOI":"10.1021\/np800121a","article-title":"Apratoxin D, a potent cytotoxic Cyclodepsipeptide from Papua New Guinea collections of the marine Cyanobacteria Lyngbya majuscula and Lyngbya sordida","volume":"71","author":"Guti\u00e9rrez","year":"2008","journal-title":"J. Nat. Prod."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1435","doi-asserted-by":"crossref","first-page":"1817","DOI":"10.3390\/md8061817","article-title":"New peptides isolated from Lyngbya species: a Review","volume":"8","author":"Liu","year":"2010","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1440","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1007\/BF01573860","article-title":"Pharmaceuticals from cultured algae","volume":"5","author":"Schwartz","year":"1990","journal-title":"J. Ind. Microbiol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1445","first-page":"3779","article-title":"Cryptophycin: a new antimicrotubule agent active against drug-resistant cells","volume":"54","author":"Smith","year":"1994","journal-title":"Cancer Res."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1450","doi-asserted-by":"crossref","first-page":"1011","DOI":"10.1021\/np9001674","article-title":"Desmethoxymajusculamide C, a cyanobacterial Depsipeptide with potent cytotoxicity in both cyclic and ring-opened forms","volume":"72","author":"Simmons","year":"2009","journal-title":"J. Nat. Prod."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1455","doi-asserted-by":"crossref","first-page":"12955","DOI":"10.18632\/oncotarget.4102","article-title":"Use of tilapia piscidin 3 (TP3) to protect against MRSA infection in mice with skin injuries","volume":"6","author":"Huang","year":"2015","journal-title":"Oncotarget"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1460","doi-asserted-by":"crossref","first-page":"1538","DOI":"10.1128\/AAC.02427-13","article-title":"Use of the antimicrobial peptide Pardaxin (GE33) to protect against methicillin-resistant Staphylococcus aureus infection in mice with skin injuries","volume":"58","author":"Huang","year":"2014","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1465","doi-asserted-by":"crossref","first-page":"11371","DOI":"10.3390\/ijms231911371","article-title":"Calcium-based antimicrobial peptide compounds attenuate DNFB-induced atopic dermatitis-like skin lesions via Th-cells in BALB\/c mice","volume":"23","author":"Liu","year":"2022","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1470","doi-asserted-by":"crossref","DOI":"10.1016\/j.pdpdt.2021.102677","article-title":"Enhancement of photodynamic bactericidal activity of curcumin against pseudomonas aeruginosa using polymyxin B","volume":"37","author":"Zhou","year":"2022","journal-title":"Photodiagn. Photodyn. Ther."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1475","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1007\/s00248-019-01385-9","article-title":"Probiotics modulate a novel amphibian skin defense peptide that is antifungal and facilitates growth of antifungal Bacteria","volume":"79","author":"Woodhams","year":"2020","journal-title":"Microb. Ecol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1480","doi-asserted-by":"crossref","DOI":"10.3389\/fmicb.2024.1390765","article-title":"Synergistic action of antimicrobial peptides and antibiotics: current understanding and future directions","volume":"15","author":"Taheri-Araghi","year":"2024","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1485","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1016\/j.resmic.2012.06.001","article-title":"Synergistic effect of antimicrobial peptide arenicin-1 in combination with antibiotics against pathogenic bacteria","volume":"163","author":"Choi","year":"2012","journal-title":"Res. Microbiol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1490","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1007\/s10517-017-3708-z","article-title":"Analysis of synergistic effects of antimicrobial peptide Arenicin-1 and conventional antibiotics","volume":"162","author":"Bolosov","year":"2017","journal-title":"Bull. Exp. Biol. Med."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1495","doi-asserted-by":"crossref","first-page":"13206","DOI":"10.1038\/s41598-020-69995-9","article-title":"Correlation between hemolytic activity, cytotoxicity and systemic in vivo toxicity of synthetic antimicrobial peptides","volume":"10","author":"Greco","year":"2020","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1500","doi-asserted-by":"crossref","DOI":"10.1002\/ctm2.822","article-title":"The role of cell-penetrating peptides in potential anti-cancer therapy","volume":"12","author":"Zhou","year":"2022","journal-title":"Clin. Transl. Med."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1505","doi-asserted-by":"crossref","first-page":"2255","DOI":"10.1007\/s00018-011-0717-3","article-title":"Beyond natural antimicrobial peptides: multimeric peptides and other peptidomimetic approaches","volume":"68","author":"Giuliani","year":"2011","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1510","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1042\/BJ20050520","article-title":"Conjugation of fatty acids with different lengths modulates the antibacterial and antifungal activity of a cationic biologically inactive peptide","volume":"390","author":"Malina","year":"2005","journal-title":"Biochem. J."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1515","doi-asserted-by":"crossref","first-page":"2699","DOI":"10.1016\/j.bbamem.2016.07.001","article-title":"Selective amino acid substitution reduces cytotoxicity of the antimicrobial peptide mastoparan","volume":"1858","author":"Irazazabal","year":"2016","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1520","doi-asserted-by":"crossref","first-page":"4870","DOI":"10.3390\/ijms25094870","article-title":"Antimicrobial peptides towards clinical application\u2014a long history to be concluded","volume":"25","author":"Cresti","year":"2024","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1525","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1111\/bcp.14130","article-title":"Food and drug administration vs European medicines agency: Review times and clinical evidence on novel drugs at the time of approval","volume":"86","author":"Joppi","year":"2020","journal-title":"Br. J. Clin. Pharmacol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1530","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1186\/s12967-025-06321-9","article-title":"Antimicrobial peptide biological activity, delivery systems and clinical translation status and challenges","volume":"23","author":"Zheng","year":"2025","journal-title":"J. Transl. Med."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1535","doi-asserted-by":"crossref","first-page":"349","DOI":"10.3390\/antibiotics11030349","article-title":"Antimicrobial peptides: from design to clinical application","volume":"11","author":"Zhang","year":"2022","journal-title":"Antibiotics"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1540","doi-asserted-by":"crossref","first-page":"840","DOI":"10.3390\/pharmaceutics12090840","article-title":"An update on antimicrobial peptides (AMPs) and their delivery strategies for wound infections","volume":"12","author":"Patrulea","year":"2020","journal-title":"Pharmaceutics"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1545","doi-asserted-by":"crossref","first-page":"15694","DOI":"10.1021\/acsomega.9b02278","article-title":"Conjugation of cell-penetrating peptides to antimicrobial peptides enhances antibacterial activity","volume":"4","author":"Lee","year":"2019","journal-title":"ACS Omega"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1550","doi-asserted-by":"crossref","first-page":"16633","DOI":"10.1074\/jbc.M115.642645","article-title":"Identification and characterization of the first cathelicidin from sea snakes with potent antimicrobial and anti-inflammatory activity and special mechanism","volume":"290","author":"Wei","year":"2015","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1555","doi-asserted-by":"crossref","first-page":"2451","DOI":"10.1021\/acsinfecdis.0c00255","article-title":"Design of a sea Snake Antimicrobial Peptide Derivative with therapeutic potential against drug-resistant bacterial infection","volume":"6","author":"Gao","year":"2020","journal-title":"ACS Infect. Dis."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1560","doi-asserted-by":"crossref","first-page":"30","DOI":"10.3390\/md18010030","article-title":"High-throughput identification of putative antimicrobial peptides from multi-omics data of the lined seahorse (Hippocampus erectus)","volume":"18","author":"Chen","year":"2019","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1565","doi-asserted-by":"crossref","first-page":"4867","DOI":"10.1093\/molbev\/msab212","article-title":"Two reference-Quality Sea Snake genomes reveal their divergent evolution of adaptive traits and venom systems","volume":"38","author":"Li","year":"2021","journal-title":"Mol. Biol. Evol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1570","doi-asserted-by":"crossref","first-page":"794","DOI":"10.3390\/antibiotics13090794","article-title":"Antimicrobial peptides and their biomedical applications: a Review","volume":"13","author":"Min","year":"2024","journal-title":"Antibiotics"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1575","first-page":"3919","article-title":"The antimicrobial peptides and their potential clinical applications","volume":"11","author":"Lei","year":"2019","journal-title":"Am. J. Transl. Res."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1580","doi-asserted-by":"crossref","first-page":"2143","DOI":"10.1021\/acsnano.0c09509","article-title":"Synthetic biology and computer-based frameworks for antimicrobial peptide discovery","volume":"15","author":"Torres","year":"2021","journal-title":"ACS Nano"},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1585","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2023.115377","article-title":"Antimicrobial peptides: structure, mechanism, and modification","volume":"255","author":"Chen","year":"2023","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1590","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1186\/s12918-017-0503-4","article-title":"Lee, identification of natural antimicrobial peptides from bacteria through metagenomic and metatranscriptomic analysis of high-throughput transcriptome data of Taiwanese oolong teas","volume":"11","author":"Huang","year":"2017","journal-title":"BMC Syst. Biol."},{"key":"10.1016\/j.ijbiomac.2025.142158_bb1595","doi-asserted-by":"crossref","first-page":"1451","DOI":"10.3390\/antibiotics11101451","article-title":"Recent Progress in the discovery and Design of Antimicrobial Peptides Using Traditional Machine Learning and Deep Learning","volume":"11","author":"Yan","year":"2022","journal-title":"Antibiotics"}],"container-title":["International Journal of Biological Macromolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813025027102?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813025027102?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,7,1]],"date-time":"2026-07-01T10:55:14Z","timestamp":1782903314000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0141813025027102"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,5]]},"references-count":319,"alternative-id":["S0141813025027102"],"URL":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2025.142158","relation":{},"ISSN":["0141-8130"],"issn-type":[{"value":"0141-8130","type":"print"}],"subject":[],"published":{"date-parts":[[2025,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Harnessing marine antimicrobial peptides for novel therapeutics: A deep dive into ocean-derived bioactives","name":"articletitle","label":"Article Title"},{"value":"International Journal of Biological Macromolecules","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2025.142158","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 Elsevier B.V. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"142158"}}