{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T21:59:26Z","timestamp":1788386366184,"version":"build-2803163510"},"reference-count":204,"publisher":"MDPI AG","issue":"7","license":[{"start":{"date-parts":[[2025,7,15]],"date-time":"2025-07-15T00:00:00Z","timestamp":1752537600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Russian Science Foundation","award":["22-14-00380-P"],"award-info":[{"award-number":["22-14-00380-P"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Marine Drugs"],"abstract":"<jats:p>Marine peptides, derived from a great number of aquatic organisms, exhibit a broad spectrum of biological activities that hold a significant therapeutic potential. This article reviews the multifaceted roles of marine peptides, focusing on their antibacterial, antibiofilm, antifungal, antiviral, antiparasitic, cytotoxic, anticancer, immunomodulatory, chemotactic, opsonizing, anti-inflammatory, antiaging, skin-protective, and wound-healing properties. By elucidating mechanisms of their action and highlighting key research findings, this review aims to provide a comprehensive understanding of possible therapeutic applications of marine peptides, underscoring their importance in developing novel drugs as well as in cosmetology, food industry, aquatic and agriculture biotechnology. Further investigations are essential to harness their therapeutic potential and should focus on detailed mechanism studies, large-scale production, and clinical evaluations with a view to confirm their efficacy and safety and translate these findings into practical applications. It is also important to investigate the potential synergistic effects of marine peptide combinations with existing medicines to enhance their efficacy. Challenges include the sustainable sourcing of marine peptides, and therefore an environmental impact of harvesting marine organisms must be considered as well.<\/jats:p>","DOI":"10.3390\/md23070288","type":"journal-article","created":{"date-parts":[[2025,7,15]],"date-time":"2025-07-15T11:52:58Z","timestamp":1752580378000},"page":"288","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":12,"title":["Multifaceted Marine Peptides and Their Therapeutic Potential"],"prefix":"10.3390","volume":"23","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6186-2462","authenticated-orcid":false,"given":"Svetlana V.","family":"Guryanova","sequence":"first","affiliation":[{"name":"M.M. Shemyakin and Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, Russia"},{"name":"Medical Institute, Peoples\u2019 Friendship University of Russia, 117198 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5950-249X","authenticated-orcid":false,"given":"Tatiana V.","family":"Ovchinnikova","sequence":"additional","affiliation":[{"name":"M.M. Shemyakin and Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, Russia"},{"name":"Moscow Center for Advanced Studies, 123592 Moscow, Russia"},{"name":"Department of Biotechnology, I.M. Sechenov First Moscow State Medical University, 119991 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,7,15]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.11646\/zootaxa.5164.1.1","article-title":"New Genera, Species and Occurrences of Deep-Sea Asteroidea (Valvatacea, Forcipulatacea, Echinodermata) collected from the North Pacific Ocean by the CAPSTONE Expedition","volume":"5164","author":"Mah","year":"2022","journal-title":"Zootaxa"},{"key":"ref_2","first-page":"zootaxa.4868.4.5","article-title":"New species of black corals (Cnidaria:Anthozoa: Antipatharia) from deep-sea seamounts and ridges in the North Pacific","volume":"4868","author":"Opresko","year":"2020","journal-title":"Zootaxa"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"191","DOI":"10.11646\/zootaxa.4012.1.11","article-title":"A new deep-sea species of the genus Urocaridella (Crustacea: Decapoda: Caridea: Palaemonidea) from Yap Seamount in the Western Pacific","volume":"4012","author":"Wang","year":"2015","journal-title":"Zootaxa"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1093\/mollus\/eyr017","article-title":"A new operational classification of the conoidea (Gastropoda)","volume":"77","author":"Bouchet","year":"2011","journal-title":"J. Molluscan Stud."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"R511","DOI":"10.1016\/j.cub.2017.04.060","article-title":"Marine Biodiversity, Biogeography, Deep-Sea Gradients, and Conservation","volume":"27","author":"Costello","year":"2017","journal-title":"Curr. Biol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1016\/j.crvi.2011.02.009","article-title":"Marine biodiversity characteristics","volume":"334","author":"Boeuf","year":"2011","journal-title":"Comptes Rendus Biol."},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"Falanga, A., Lombardi, L., Franci, G., Vitiello, M., Iovene, M.R., Morelli, G., Galdiero, M., and Galdiero, S. (2016). Marine Antimicrobial Peptides: Nature Provides Templates for the Design of Novel Compounds against Pathogenic Bacteria. Int. J. Mol. Sci., 17.","DOI":"10.3390\/ijms17050785"},{"key":"ref_8","doi-asserted-by":"crossref","unstructured":"Ovchinnikova, T.V. (2019). Structure, Function, and Therapeutic Potential of Marine Bioactive Peptides. Mar. Drugs, 17.","DOI":"10.3390\/md17090505"},{"key":"ref_9","doi-asserted-by":"crossref","unstructured":"Ovchinnikova, T.V. (2021). Marine Peptides: Structure, Bioactivities, and a New Hope for Therapeutic Application. Mar. Drugs, 19.","DOI":"10.3390\/md19080407"},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Guryanova, S.V., Gigani, O.B., Gudima, G.O., Kataeva, A.M., and Kolesnikova, N.V. (2022). Dual Effect of Low-Molecular-Weight Bioregulators of Bacterial Origin in Experimental Model of Asthma. Life, 12.","DOI":"10.3390\/life12020192"},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Guryanova, S.V. (2022). Regulation of Immune Homeostasis via Muramyl Peptides-Low Molecular Weight Bioregulators of Bacterial Origin. Microorganisms, 10.","DOI":"10.3390\/microorganisms10081526"},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Guryanova, S.V., and Kataeva, A. (2023). Inflammation Regulation by Bacterial Molecular Patterns. Biomedicines, 11.","DOI":"10.3390\/biomedicines11010183"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"470","DOI":"10.22363\/2313-0245-2023-27-4-470-482","article-title":"Mechanisms of regulation allergic and autoimmune reactions by bacterial origin bioregulators","volume":"27","author":"Guryanova","year":"2023","journal-title":"RUDN J. Med."},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Guryanova, S.V. (2024). Bacteria and Allergic Diseases. Int. J. Mol. Sci., 25.","DOI":"10.20944\/preprints202408.1342.v1"},{"key":"ref_15","first-page":"365","article-title":"Influence of muramyl peptides on the production of chemokines, growth factors, pro-inflammatory and anti-inflammatory cytokines","volume":"28","author":"Guryanova","year":"2024","journal-title":"RUDN J. Med."},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Chi, C.-F., and Wang, B. (2023). Marine Bioactive Peptides\u2014Structure, Function and Application. Mar. Drugs, 21.","DOI":"10.3390\/books978-3-0365-8261-0"},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Ovchinnikova, T.V., and Shi, Q. (2023). Aquatic genomics and transcriptomics for evolutionary biology. Front. Genet. Sec. Evol. Popul. Genet., 14.","DOI":"10.3389\/fgene.2023.1183637"},{"key":"ref_18","doi-asserted-by":"crossref","unstructured":"Pangestuti, R., and Kim, S.-K. (2017). Bioactive Peptide of Marine Origin for the Prevention and Treatment of Non-Communicable Diseases. Mar. Drugs, 15.","DOI":"10.3390\/md15030067"},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Zhang, Q.-T., Liu, Z.-D., Wang, Z., Wang, T., Wang, N., Wang, N., Zhang, B., and Zhao, Y.-F. (2021). Recent Advances in Small Peptides of Marine Origin in Cancer Therapy. Mar. Drugs, 19.","DOI":"10.3390\/md19020115"},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Sukmarini, L. (2022). Antiviral Peptides (AVPs) of Marine Origin as Propitious Therapeutic Drug Candidates for the Treatment of Human Viruses. Molecules, 27.","DOI":"10.3390\/molecules27092619"},{"key":"ref_21","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":"ref_22","doi-asserted-by":"crossref","unstructured":"Guryanova, S.V., and Ovchinnikova, T.V. (2022). Innate Immunity Mechanisms in Marine Multicellular Organisms. Mar. Drugs, 20.","DOI":"10.3390\/md20090549"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"110468","DOI":"10.1016\/j.foodres.2021.110468","article-title":"Recent developments on production, purification and biological activity of marine peptides","volume":"147","author":"Sridhar","year":"2021","journal-title":"Food Res. Int."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"867","DOI":"10.1016\/j.procbio.2015.02.012","article-title":"In Vitro Antiviral Activities of Enzymatic Hydrolysates Extracted from Byproducts of the Atlantic Holothurian Cucumaria frondosa","volume":"50","author":"Tripoteau","year":"2015","journal-title":"Process Biochem."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1486","DOI":"10.1016\/j.procbio.2007.07.016","article-title":"Optimization of free radical scavenging activity by response surface methodology in the hydrolysis of shrimp processing discards","volume":"42","author":"Guerard","year":"2007","journal-title":"Process Biochem."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1724","DOI":"10.2174\/0929867324666170424124416","article-title":"A therapeutic potential of animal \u03b2-hairpin antimicrobial peptides","volume":"24","author":"Panteleev","year":"2017","journal-title":"Curr. Med. Chem."},{"key":"ref_27","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 jellifish Aurelia aurita","volume":"429","author":"Shenkarev","year":"2012","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"5565","DOI":"10.1039\/D0FO00530D","article-title":"In silico evaluation of marine fish proteins as nutritional supplements for COVID-19 patients","volume":"11","author":"Yao","year":"2020","journal-title":"Food Funct."},{"key":"ref_29","doi-asserted-by":"crossref","unstructured":"Ovchinnikova, T.V., and Shi, Q. (2023). Omics-based identification, characterization, and validation of marine bioactive peptides. Front. Mar. Sci., 10.","DOI":"10.3389\/fmars.2023.1323847"},{"key":"ref_30","doi-asserted-by":"crossref","unstructured":"Panteleev, P.V., Safronova, V.N., Duan, S., Komlev, A.S., Bolosov, I.A., Kruglikov, R.N., Kombarova, T.I., Korobova, O.V., Pereskokova, E.S., and Borzilov, A.I. (2023). Novel BRICHOS-related antimicrobial peptides from the marine worm Heteromastus filiformis: Transcriptome mining, synthesis, biological activities, and therapeutic potential. Mar. Drugs, 21.","DOI":"10.3390\/md21120639"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"109546","DOI":"10.1016\/j.fsi.2024.109546","article-title":"Histone derived antimicrobial peptides identified from Mytilus coruscus serum by peptidomics","volume":"149","author":"Wang","year":"2024","journal-title":"Fish Shellfish Immunol."},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Fidor, A., Konkel, R., and Mazur-Marzec, H. (2019). Bioactive peptides produced by cyanobacteria of the genus Nostoc. Mar. Drugs, 17.","DOI":"10.3390\/md17100561"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"618","DOI":"10.3390\/md13010618","article-title":"Marine peptides and their anti-infective activities","volume":"13","author":"Kang","year":"2015","journal-title":"Mar. Drugs"},{"key":"ref_34","doi-asserted-by":"crossref","unstructured":"Wen, Q., Liu, R., Ouyang, Z., He, T., Zhang, W., and Chen, X. (2022). Identification of a new antifungal peptide W1 from a marine Bacillus amyloliquefaciens reveals its potential in controlling fungal plant diseases. Front. Microbiol., 13.","DOI":"10.3389\/fmicb.2022.922454"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"134419","DOI":"10.1016\/j.foodchem.2022.134419","article-title":"Epinecidin-1, a marine antifungal peptide, inhibits Botrytis cinerea and delays gray mold in postharvest peaches","volume":"403","author":"Fan","year":"2023","journal-title":"Food Chem."},{"key":"ref_36","doi-asserted-by":"crossref","unstructured":"Solov\u2019eva, T.F., Bakholdina, S.I., and Naberezhnykh, G.A. (2023). Host defense proteins and peptides with lipopolysaccharide-binding activity from marine invertebrates and their therapeutic potential in Gram-negative sepsis. Mar. Drugs, 21.","DOI":"10.20944\/preprints202309.1583.v1"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/j.febslet.2004.10.012","article-title":"Purification and primary structure of two isoforms of arenicin, a novel antimicrobial peptide from marine polychaeta Arenicola marina","volume":"577","author":"Ovchinnikova","year":"2004","journal-title":"FEBS Lett."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1002\/bip.20865","article-title":"Molecular insight into mechanism of antimicrobial action of the beta-hairpin peptide arenicin: Specific oligomerization in detergent micelles","volume":"5","author":"Ovchinnikova","year":"2008","journal-title":"Biopolymers"},{"key":"ref_39","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":"ref_40","doi-asserted-by":"crossref","first-page":"e23093","DOI":"10.1002\/bip.23093","article-title":"Marine antimicrobial peptide arenicin adopts a monomeric twisted \u03b2-hairpin structure and forms low conductivity pores in zwitterionic lipid bilayers","volume":"110","author":"Sychev","year":"2017","journal-title":"Pept. Sci."},{"key":"ref_41","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":"2015","journal-title":"J. Pept. Sci."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/bs.vh.2019.01.011","article-title":"Hepcidin, iron, and bacterial infection","volume":"110","author":"Barton","year":"2019","journal-title":"Vitam. Horm."},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Gong, R., An, Z., Zhang, W., Chen, F., and Wang, K.-J. (2022). The antimicrobial peptide LJ-hep2 from Lateolabrax japonicus exerting activities against multiple pathogenic bacteria and immune protection in vivo. Mar. Drugs, 20.","DOI":"10.3390\/md20100651"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"6319","DOI":"10.3390\/molecules20046319","article-title":"Insights into the antimicrobial properties of hepcidins: Advantages and drawbacks as potential therapeutic agents","volume":"20","author":"Lombardi","year":"2015","journal-title":"Molecules"},{"key":"ref_45","doi-asserted-by":"crossref","unstructured":"Chen, R.-C., and Lan, C.-Y. (2020). Human antimicrobial peptide hepcidin 25-induced apoptosis in Candida albicans. Microorganisms, 8.","DOI":"10.3390\/microorganisms8040585"},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Nemeth, E., and Ganz, T. (2021). Hepcidin-ferroportin interaction controls systemic iron homeostasis. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22126493"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/bs.vh.2019.01.002","article-title":"Hepcidin-ferroportin axis in health and disease","volume":"110","author":"Ginzburg","year":"2019","journal-title":"Vitam. Horm."},{"key":"ref_48","doi-asserted-by":"crossref","unstructured":"Safronova, V.N., Panteleev, P.V., Sukhanov, S.V., Toropygin, I.Y., Bolosov, I.A., and Ovchinnikova, T.V. (2022). Mechanism of action and therapeutic potential of the beta-hairpin antimicrobial peptide capitellacin from the marine polychaeta Capitella teleta. Mar. Drugs, 20.","DOI":"10.3390\/md20030167"},{"key":"ref_49","doi-asserted-by":"crossref","unstructured":"Safronova, V.N., Bolosov, I.A., Kruglikov, R.N., Korobova, O.V., Pereskokova, E.S., Borzilov, A.I., Panteleev, P.V., and Ovchinnikova, T.V. (2022). Novel \u03b2-hairpin peptide from marine polychaeta with a high efficacy against Gram-negative pathogens. Mar. Drugs, 20.","DOI":"10.3390\/md20080517"},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"Panteleev, P.V., Tsarev, A.V., Safronova, V.N., Reznikova, O.V., Bolosov, I.A., Sychev, S.V., Shenkarev, Z.O., and Ovchinnikova, T.V. (2020). Structure elucidation and functional studies of a novel \u03b2-hairpin antimicrobial peptide from the marine polychaeta Capitella teleta. Mar. Drugs, 18.","DOI":"10.3390\/md18120620"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"13546","DOI":"10.1074\/jbc.M211332200","article-title":"Plicatamide, an antimicrobial octapeptide from Styela plicata hemocytes","volume":"278","author":"Tincu","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/S0014-5793(02)02827-2","article-title":"Halocidin: A new antimicrobial peptide from hemocytes of the solitary tunicate, Halocynthia aurantium","volume":"521","author":"Jang","year":"2002","journal-title":"FEBS Lett."},{"key":"ref_53","doi-asserted-by":"crossref","unstructured":"Franchi, N., Ballarin, L., and Cima, F. (2023). Botryllin, a novel antimicrobial peptide from the colonial ascidian Botryllus schlosseri. Mar. Drugs, 21.","DOI":"10.3390\/md21020074"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1007\/s11094-017-1518-2","article-title":"Effect of arenicins and other beta-hairpin antimicrobial peptides on Pseudomonas aeruginosa PAI1 biofilms","volume":"50","author":"Panteleev","year":"2017","journal-title":"Pharm. Chem. J."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1007\/s00253-009-1987-7","article-title":"Anti-adhesion activity of two biosurfactants produced by Bacillus spp. prevents biofilm formation of human bacterial pathogens","volume":"83","author":"Rivardo","year":"2009","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_56","doi-asserted-by":"crossref","unstructured":"Muras, A., Larroze, S., Mayer, C., Teixeira, T., Wengier, R., Benayahu, Y., and Otero, A. (2021). Evaluation of the anti-fouling efficacy of Bacillus licheniformis extracts under environmental and natural conditions. Front. Mar. Sci., 8.","DOI":"10.3389\/fmars.2021.711108"},{"key":"ref_57","doi-asserted-by":"crossref","unstructured":"Muras, A., L\u00f3pez-P\u00e9rez, M., Mayer, C., Parga, A., Amaro-Blanco, J., and Otero, A. (2018). High prevalence of quorum-sensing and quorum-quenching activity among cultivable bacteria and metagenomic sequences in the Mediterranean Sea. Genes, 9.","DOI":"10.3390\/genes9020100"},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Soler, A., Arregui, L., Arroyo, M., Mendoza, J.A., Muras, A., and \u00c1lvarez, C. (2018). Quorum sensing versus quorum quenching bacterial isolates obtained from MBR plants treating leachates from municipal solid waste. Int. J. Environ. Res. Public Health, 15.","DOI":"10.3390\/ijerph15051019"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1111\/j.1749-6632.1988.tb40395.x","article-title":"Antifungal substances from marine invertebrates","volume":"544","author":"Fusetani","year":"1988","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"649","DOI":"10.2174\/1385272802666220130083412","article-title":"Antifungal metabolites from marine sponges","volume":"2","author":"Li","year":"1998","journal-title":"Curr. Org. Chem."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"16709","DOI":"10.1016\/S0021-9258(18)37448-9","article-title":"Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure","volume":"263","author":"Nakamura","year":"1988","journal-title":"J. Biol. Chem."},{"key":"ref_62","first-page":"53","article-title":"Antifungal peptides in marine invertebrates","volume":"7","author":"Fusetani","year":"2010","journal-title":"Invertebr. Surviv. J."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"2961","DOI":"10.1128\/AAC.42.11.2961","article-title":"Specific activities of dolastatin 10 and peptide derivatives against Cryptococcus neoformans","volume":"42","author":"Pettit","year":"1998","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"907","DOI":"10.1021\/np010049y","article-title":"Isolation of dolastatin 10 from the marine cyanobacterium Symploca species VP642 and total stereochemistry and biological evaluation of its analogue symplostatin 1","volume":"64","author":"Luesch","year":"2001","journal-title":"J. Nat. Prod."},{"key":"ref_65","doi-asserted-by":"crossref","unstructured":"Gao, G., Wang, Y., Hua, H., Li, D., and Tang, C. (2021). Marine antitumor peptide dolastatin 10: Biological activity, structural modification and synthetic chemistry. Mar. Drugs, 19.","DOI":"10.3390\/md19070363"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"4340","DOI":"10.1021\/jm061288r","article-title":"Lysosome and HER3 (ErbB3) selective anticancer agent kahalalide F: Semisynthetic modifications and antifungal lead-exploration studies","volume":"50","author":"Shilabin","year":"2007","journal-title":"J. Med. Chem."},{"key":"ref_67","doi-asserted-by":"crossref","unstructured":"Thawabteh, A.M., Swaileh, Z., Ammar, M., Jaghama, W., Yousef, M., Karaman, R.A., Bufo, S., and Scrano, L. (2023). Antifungal and antibacterial activities of isolated marine compounds. Toxins, 15.","DOI":"10.3390\/toxins15020093"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1021\/np049671r","article-title":"Hassallidin A, a glycosylated lipopeptide with antifungal activity from the cyanobacterium Hassallia sp.","volume":"68","author":"Neuhof","year":"2005","journal-title":"J. Nat. Prod."},{"key":"ref_69","doi-asserted-by":"crossref","unstructured":"Watson, A., Agius, J., Ackerly, D., Beddoe, T., and Helbig, K. (2022). The Role of anti-viral effector molecules in mollusc hemolymph. Biomolecules, 12.","DOI":"10.3390\/biom12030345"},{"key":"ref_70","first-page":"100006","article-title":"Bioactives from marine resources as natural health products: A review","volume":"77","author":"Santhiravel","year":"2025","journal-title":"Pharmacol. Rev."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1016\/j.fsi.2017.12.018","article-title":"A single WAP domain (SWD)-containing protein with antiviral activity from pacific white shrimp Litopenaeus vannamei","volume":"73","author":"Yang","year":"2018","journal-title":"Fish Shellfish Immunol."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"7692","DOI":"10.1128\/JVI.00591-16","article-title":"Antiviral activity of myticin C peptide from mussel: An ancient defense against herpesviruses","volume":"90","author":"Novoa","year":"2016","journal-title":"J. Virol."},{"key":"ref_73","doi-asserted-by":"crossref","unstructured":"Zannella, C., Mosca, F., Mariani, F., Franci, G., Folliero, V., Galdiero, M., Tiscar, P.G., and Galdiero, M. (2017). Microbial diseases of bivalve mollusks: Infections, immunology and antimicrobial defense. Mar. Drugs, 15.","DOI":"10.3390\/md15060182"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1016\/j.fsi.2009.02.001","article-title":"Functional and molecular immune response of Mediterranean mussel (Mytilus galloprovincialis) haemocytes against pathogen-associated molecular patterns and bacteria","volume":"26","author":"Costa","year":"2009","journal-title":"Fish Shellfish Immunol."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1016\/j.dci.2008.08.005","article-title":"Evidence of high individual diversity on myticin C in mussel (Mytilus galloprovincialis)","volume":"33","author":"Costa","year":"2009","journal-title":"Dev. Comp. Immunol."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"1521","DOI":"10.1128\/AAC.41.7.1521","article-title":"Discovery of cyanovirin-N, a novel human immunodeficiency virus-inactivating protein that binds viral surface envelope glycoprotein gp120: Potential applications to microbicide development","volume":"41","author":"Boyd","year":"1997","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.antiviral.2018.02.017","article-title":"Inhibition of NF-\u03baB-dependent HIV-1 replication by the marine natural product bengamide A","volume":"152","author":"Tietjen","year":"2018","journal-title":"Antivir. Res."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"740","DOI":"10.1021\/acs.jnatprod.6b00970","article-title":"The bengamides: A mini-review of natural sources, analogues, biological properties, biosynthetic origins, and future prospects","volume":"80","author":"White","year":"2017","journal-title":"J. Nat. Prod."},{"key":"ref_79","doi-asserted-by":"crossref","unstructured":"Porras-Alcal\u00e1, C., Moya-Utrera, F., Garc\u00eda-Castro, M., S\u00e1nchez-Ruiz, A., L\u00f3pez-Romero, J.M., Pino-Gonz\u00e1lez, M.S., D\u00edaz-Morilla, A., Kitamura, S., Wolan, D.W., and Prados, J. (2022). The development of the bengamides as new antibiotics against drug-resistant bacteria. Mar. Drugs, 20.","DOI":"10.3390\/md20060373"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"4215","DOI":"10.1016\/j.tetlet.2015.05.058","article-title":"Stellettapeptins A and B, HIV-inhibitory cyclic depsipeptides from the marine sponge Stelletta sp.","volume":"56","author":"Shin","year":"2015","journal-title":"Tetrahedron Lett."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1134\/S1068162010061019","article-title":"Isolation and structure of a novel peptide inhibitor of HIV-1 integrase from marine polychaetes","volume":"37","author":"Elyakova","year":"2011","journal-title":"Russ. J. Bioorg. Chem."},{"key":"ref_82","doi-asserted-by":"crossref","unstructured":"Festa, M., Sansone, C., Brunet, C., Crocetta, F., Di Paola, L., Lombardo, M., Bruno, A., Noonan, D.M., and Albini, A. (2020). Cardiovascular Active Peptides of Marine Origin with ACE Inhibitory Activities: Potential Role as Anti-Hypertensive Drugs and in Prevention of SARSCoV-2 Infection. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21218364"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"102331","DOI":"10.1016\/j.algal.2021.102331","article-title":"Viral Inhibitors Derived from Macroalgae, Microalgae, and Cyanobacteria: A Review of Antiviral Potential throughout Pathogenesis","volume":"57","author":"Reynolds","year":"2021","journal-title":"Algal Res."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"926","DOI":"10.1126\/science.abf4058","article-title":"Plitidepsin Has Potent Preclinical Efficacy against SARS-CoV-2 by Targeting the Host Protein EEF1A","volume":"371","author":"White","year":"2021","journal-title":"Science"},{"key":"ref_85","first-page":"8204","article-title":"Didemnins Inhibit COVID-19 Main Protease (MPRO)","volume":"11","author":"Sahin","year":"2021","journal-title":"Biointerface Res. Appl. Chem."},{"key":"ref_86","doi-asserted-by":"crossref","unstructured":"Gentile, D., Patamia, V., Scala, A., Sciortino, M.T., Piperno, A., and Rescifina, A. (2020). Putative Inhibitors of SARS-CoV-2 Main Protease from a Library of Marine Natural Products: A Virtual Screening and Molecular Modeling Study. Mar. Drugs, 18.","DOI":"10.20944\/preprints202003.0372.v1"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"2956","DOI":"10.1021\/acs.jmedchem.1c01494","article-title":"Potent Anti-SARS-CoV-2 Activity by the Natural Product Gallinamide A and Analogues via Inhibition of Cathepsin L","volume":"65","author":"Ashhurst","year":"2022","journal-title":"J. Med. Chem."},{"key":"ref_88","doi-asserted-by":"crossref","unstructured":"Ribeiro, R., Costa, L., Pinto, E., Sousa, E., and Fernandes, C. (2023). Therapeutic Potential of Marine-Derived Cyclic Peptides as Antiparasitic Agents. Mar. Drugs, 21.","DOI":"10.3390\/md21120609"},{"key":"ref_89","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":"ref_90","doi-asserted-by":"crossref","first-page":"1154","DOI":"10.1128\/AAC.32.8.1154","article-title":"New class of antifungal agents: Jasplakinolide, a cyclodepsipeptide from the marine sponge, Jaspis species","volume":"32","author":"Scott","year":"1988","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"14869","DOI":"10.1016\/S0021-9258(17)36545-6","article-title":"Jasplakinolide, a cytotoxic natural product, induces actin polymerization and competitively inhibits the binding of phalloidin to F-actin","volume":"269","author":"Bubb","year":"1994","journal-title":"J. Biol. Chem."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"5163","DOI":"10.1074\/jbc.275.7.5163","article-title":"Effects of jasplakinolide on the kinetics of actin polymerization. An explanation for certain in vivo observations","volume":"275","author":"Bubb","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_93","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":"ref_94","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1016\/S1286-4579(99)80066-5","article-title":"Toxoplasma gondii motility and host cell invasiveness are drastically impaired by jasplakinolide, a cyclic peptide stabilizing F-actin","volume":"1","author":"Poupel","year":"1999","journal-title":"Microbes Infect."},{"key":"ref_95","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":"ref_96","doi-asserted-by":"crossref","first-page":"2433","DOI":"10.1002\/cbic.201500472","article-title":"Gift from Nature: Cyclomarin A Kills Mycobacteria and Malaria Parasites by Distinct Modes of Action","volume":"16","author":"Roggo","year":"2015","journal-title":"ChemBioChem"},{"key":"ref_97","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":"ref_98","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":"ref_99","first-page":"41","article-title":"Potensi Antelmintika Ekstrak Bakteri Simbion Spons Laut Terhadap Trichostrongylidae (Nematoda) Parasit Domba","volume":"21","author":"Faisal","year":"2017","journal-title":"J. Ilmu Pertan. Indones."},{"key":"ref_100","doi-asserted-by":"crossref","unstructured":"Kang, H.K., Lee, H.H., Seo, C.H., and Park, Y. (2019). Antimicrobial and Immunomodulatory Properties and Applications of Marine-Derived Proteins and Peptides. Mar. Drugs, 17.","DOI":"10.3390\/md17060350"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"1525","DOI":"10.1021\/ol070294u","article-title":"Thalassospiramides A and B, immunosuppressive peptides from the marine bacterium Thalassospira sp.","volume":"9","author":"Oh","year":"2007","journal-title":"Org. Lett."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"611","DOI":"10.3390\/md11030611","article-title":"Thalassospiramide G, a new gamma-amino-acid-bearing peptide from the marine bacterium Thalassospira sp.","volume":"11","author":"Um","year":"2013","journal-title":"Mar. Drugs"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"1701","DOI":"10.3892\/ijmm.2015.2386","article-title":"Bioactive peptide from Pyropia yezoensis and its anti-inflammatory activities","volume":"36","author":"Lee","year":"2015","journal-title":"Int. J. Mol. Med."},{"key":"ref_104","doi-asserted-by":"crossref","unstructured":"Garc\u00eda-Beltr\u00e1n, J.M., Arizcun, M., and Chaves-Pozo, E. (2023). Antimicrobial Peptides from Photosynthetic Marine Organisms with Potential Application in Aquaculture. Mar. Drugs, 21.","DOI":"10.3390\/md21050290"},{"key":"ref_105","doi-asserted-by":"crossref","unstructured":"Zhao, R., Jiang, X.-X., Zhao, Q.-L., Ye, H.-W., Lin, Y., Huang, J., and Tang, Y.-P. (2022). Immunoenhancing Effects of Cyclina sinensis Pentadecapeptide through Modulation of Signaling Pathways in Mice with Cyclophosphamide-Induced Immunosuppression. Mar. Drugs, 20.","DOI":"10.3390\/md20090560"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"10968","DOI":"10.1039\/D0FO02497J","article-title":"Macrophage-stimulating activity of European eel (Anguilla anguilla) peptides in RAW264.7 cells mediated via NF-\u03baB and MAPK signaling pathways","volume":"11","author":"Yao","year":"2020","journal-title":"Food Funct."},{"key":"ref_107","doi-asserted-by":"crossref","unstructured":"Hayes, M., Naik, A., Mora, L., I\u00f1arra, B., Ibarruri, J., Bald, C., Cariou, T., Reid, D., Gallagher, M., and Drag\u00f8y, R. (2024). Generation, Characterisation and Identification of Bioactive Peptides from Mesopelagic Fish Protein Hydrolysates Using In Silico and In Vitro Approaches. Mar. Drugs, 22.","DOI":"10.20944\/preprints202406.0018.v1"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1007\/s10989-025-10708-z","article-title":"Protective Effects of KC14 Peptide from Cyprinus carpio on Copper Sulfate-Induced Toxicity in Zebrafish Larvae: Insights into Anti-inflammatory Cytokine and Glutathione Modulations","volume":"31","author":"Vijayanand","year":"2025","journal-title":"Int. J. Pept. Res. Ther."},{"key":"ref_109","doi-asserted-by":"crossref","unstructured":"Khatun, M.S., Hasan, M.M., and Kurata, H. (2019). PreAIP: Computational Prediction of Anti-inflammatory Peptides by Integrating Multiple Complementary Features. Front. Genet., 10.","DOI":"10.3389\/fgene.2019.00129"},{"key":"ref_110","doi-asserted-by":"crossref","unstructured":"Umnyakova, E.S., Gorbunov, N.P., Zhakhov, A.V., Krenev, I.A., Ovchinnikova, T.V., Kokryakov, V.N., and Berlov, M.N. (2018). Modulation of Human Complement System by Antimicrobial Peptide Arenicin-1 from Arenicola marina. Mar. Drugs, 16.","DOI":"10.3390\/md16120480"},{"key":"ref_111","doi-asserted-by":"crossref","unstructured":"Krenev, I.A., Umnyakova, E.S., Eliseev, I.E., Dubrovskii, Y.A., Gorbunov, N.P., Pozolotin, V.A., Komlev, A.S., Panteleev, P.V., Balandin, S.V., and Ovchinnikova, T.V. (2020). Antimicrobial Peptide Arenicin-1 Derivative Ar-1-(C\/A) as Complement System Modulator. Mar. Drugs, 18.","DOI":"10.3390\/md18120631"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1134\/S1068162015060035","article-title":"Interaction of Arenicin-1 with C1q Protein","volume":"41","author":"Berlov","year":"2015","journal-title":"Russ. J. Bioorg. Chem."},{"key":"ref_113","doi-asserted-by":"crossref","unstructured":"Krenev, I.A., Panteleev, P.V., Umnyakova, E.S., Gorbunov, N.P., Kostevich, V.A., Balandin, S.V., Ovchinnikova, T.V., Aleshina, G.M., and Berlov, M.N. (2022). In Vitro Modulation of Complement Activation by Therapeutically Prospective Analogues of the Marine Polychaeta Arenicin Peptides. Mar. Drugs, 20.","DOI":"10.3390\/md20100612"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"105144","DOI":"10.1016\/j.dci.2024.105144","article-title":"The effects of four paralogous piscidin antimicrobial peptides on the chemotaxis, macrophage respiratory burst, phagocytosis and expression of immune-related genes in orange-spotted grouper (Epinephelus coicodes)","volume":"154","author":"Huang","year":"2024","journal-title":"Dev. Comp. Immunol."},{"key":"ref_115","doi-asserted-by":"crossref","unstructured":"Zaccone, G., Capillo, G., Fernandes, J.M.O., Kiron, V., Lauriano, E.R., Alesci, A., Lo Cascio, P., Guerrera, M.C., Kuciel, M., and Zuwala, K. (2022). Expression of the Antimicrobial Peptide Piscidin 1 and Neuropeptides in Fish Gill and Skin: A Potential Participation in Neuro-Immune Interaction. Mar. Drugs, 20.","DOI":"10.3390\/md20020145"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/j.fsi.2012.10.009","article-title":"Crustin, a Wap Domain Containing Antimicrobial Peptide from Freshwater Prawn Macrobrachium rosenbergii: Immune Characterization","volume":"34","author":"Arockiaraj","year":"2013","journal-title":"Fish Shellfish Immunol."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"1049","DOI":"10.1016\/j.dci.2009.05.006","article-title":"Characterization of Crustin Antimicrobial Proteins from Japanese Spiny Lobster Panulirus japonicus","volume":"33","author":"Pisuttharachai","year":"2009","journal-title":"Dev. Comp. Immunol."},{"key":"ref_118","doi-asserted-by":"crossref","unstructured":"Barreto, C., Coelho, J.D.R., Yuan, J., Xiang, J., Perazzolo, L.M., and Rosa, R.D. (2018). Specific Molecular Signatures for Type II Crustins in Penaeid Shrimp Uncovered by the Identification of Crustin-Like Antimicrobial Peptides in Litopenaeus vannamei. Mar. Drugs, 16.","DOI":"10.3390\/md16010031"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/j.dci.2007.04.004","article-title":"Cloning, Expression and Antimicrobial Activity of CrustinPm1, a Major Isoform of Crustin, From the Black Tiger Shrimp Penaeus monodon","volume":"32","author":"Supungul","year":"2008","journal-title":"Dev. Comp. Immunol."},{"key":"ref_120","doi-asserted-by":"crossref","unstructured":"Jiang, M., Chen, R., Chen, F., Zhu, X., and Wang, K.J. (2022). A New Crustin Gene Homolog SpCrus8 Identified in Scylla paramamosain Exerting In Vivo Protection Through Opsonization and Immunomodulation. Front. Immunol., 13.","DOI":"10.3389\/fimmu.2022.946227"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1016\/j.fsi.2013.04.035","article-title":"A Single Whey Acidic Protein Domain Containing Protein (Swd) Inhibits Bacteria Invasion and Dissemination in Shrimp Marsupenaeus japonicus","volume":"35","author":"Jiang","year":"2013","journal-title":"Fish Shellfish Immunol."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1016\/j.dci.2014.11.021","article-title":"A Novel Crustin from Marsupenaeus japonicus Promotes Hemocyte Phagocytosis","volume":"49","author":"Liu","year":"2015","journal-title":"Dev. Comp. Immunol."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"668","DOI":"10.1016\/j.dci.2008.11.010","article-title":"The role of crustins in Litopenaeus vannamei in response to infection with shrimp pathogens: An in vivo approach","volume":"33","author":"Shockey","year":"2009","journal-title":"Dev. Comp. Immunol."},{"key":"ref_124","doi-asserted-by":"crossref","unstructured":"Calcabrini, C., Catanzaro, E., Bishayee, A., Turrini, E., and Fimognari, C. (2017). Marine Sponge Natural Products with Anticancer Potential: An Updated Review. Mar. Drugs, 15.","DOI":"10.3390\/md15100310"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1111\/bph.14876","article-title":"Enriching cancer pharmacology with drugs of marine origin","volume":"177","author":"Jimenez","year":"2020","journal-title":"Br. J. Pharmacol."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1093\/jnci\/85.6.483","article-title":"Growth inhibition of human lymphoma cell lines by the marine products, dolastatins 10 and 15","volume":"85","author":"Beckwith","year":"1993","journal-title":"J. Natl. Cancer Inst."},{"key":"ref_127","doi-asserted-by":"crossref","unstructured":"Ahmed, S., Aschner, M., Alsharif, K.F., Allahyani, M., Huang, G., Wan, C., and Khan, H. (Naunyn Schmiedebergs Arch. Pharmacol., 2025). Marine peptides in lymphoma: Surgery at molecular level for therapeutic understanding, Naunyn Schmiedebergs Arch. Pharmacol., ahead of print.","DOI":"10.1007\/s00210-025-03901-w"},{"key":"ref_128","first-page":"1021","article-title":"Dolastatin 15 induces apoptosis and BCL-2 phosphorylation in small cell lung cancer cell lines","volume":"18","author":"Ali","year":"1998","journal-title":"Anticancer Res."},{"key":"ref_129","doi-asserted-by":"crossref","unstructured":"Gong, F., Chen, M.-F., Zhang, Y.-Y., Li, C.-Y., Zhou, C.-X., Hong, P.-Z., Sun, S.-L., and Qian, Z.-J. (2019). A Novel Peptide from Abalone (Haliotis discus hannai) to Suppress Metastasis and Vasculogenic Mimicry of Tumor Cells and Enhance Anti-Tumor Effect In Vitro. Mar. Drugs, 17.","DOI":"10.3390\/md17040244"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1007\/s002800050564","article-title":"Cytotoxic peptides hemiasterlin, hemiasterlin A and hemiasterlin B induce mitotic arrest and abnormal spindle formation","volume":"39","author":"Anderson","year":"1997","journal-title":"Cancer Chemother. Pharmacol."},{"key":"ref_131","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":"ref_132","doi-asserted-by":"crossref","first-page":"809","DOI":"10.1111\/cbdd.13810","article-title":"Tachyplesin induces apoptosis in non-small cell lung cancer cells and enhances the chemosensitivity of A549\/DDP cells to cisplatin by activating Fas and necroptosis pathway","volume":"97","author":"Wu","year":"2021","journal-title":"Chem. Biol. Drug Des."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1007\/s10517-018-4134-6","article-title":"In Vitro Study of Antitumor Effect of Antimicrobial Peptide Tachyplesin I in Combination with Cisplatin","volume":"165","author":"Kuzmin","year":"2018","journal-title":"Bull. Exp. Biol. Med."},{"key":"ref_134","doi-asserted-by":"crossref","unstructured":"Guryanova, S.V., Balandin, S.V., Belogurova-Ovchinnikova, O.Y., and Ovchinnikova, T.V. (2023). Marine Invertebrate Antimicrobial Peptides and Their Potential as Novel Peptide Antibiotics. Mar. Drugs, 21.","DOI":"10.3390\/md21100503"},{"key":"ref_135","doi-asserted-by":"crossref","unstructured":"Marggraf, M.B., Panteleev, P.V., Emelianova, A.A., Sorokin, M.I., Bolosov, I.A., Buzdin, A.A., Kuzmin, D.V., and Ovchinnikova, T.V. (2018). Cytotoxic potential of the novel horseshoe crab peptide polyphemusin III. Mar. Drugs, 16.","DOI":"10.3390\/md16120466"},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"933","DOI":"10.1126\/science.7233187","article-title":"Didemnins: Antiviral and antitumor depsipeptides from a caribbean tunicate","volume":"212","author":"Kuentzel","year":"1981","journal-title":"Science"},{"key":"ref_137","first-page":"87","article-title":"Antiviral and antitumor compounds from tunicates","volume":"42","author":"Rinehart","year":"1983","journal-title":"Fed. Proc."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"9177","DOI":"10.1021\/bi00028a030","article-title":"Mechanism of protein synthesis inhibition by didemnin B in vitro","volume":"34","author":"SirDeshpande","year":"1995","journal-title":"Biochemistry"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"4339","DOI":"10.1021\/bi992202h","article-title":"Inhibition of protein synthesis by didemnin B: How EF-1alpha mediates inhibition of translocation","volume":"39","author":"Ahuja","year":"2000","journal-title":"Biochemistry"},{"key":"ref_140","first-page":"333","article-title":"Effect of dehydrodidemnin B on human colon carcinoma cell lines","volume":"17","author":"Lobo","year":"1997","journal-title":"Anticancer Res."},{"key":"ref_141","first-page":"1389","article-title":"A Quick Guide to Small-Molecule Inhibitors of Eukaryotic Protein Synthesis","volume":"85","author":"Dmitriev","year":"2020","journal-title":"Biochemistry"},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1016\/j.freeradbiomed.2024.04.235","article-title":"Marine-derived antimicrobial peptide piscidin-1 triggers extrinsic and intrinsic apoptosis in oral squamous cell carcinoma through reactive oxygen species production and inhibits angiogenesis","volume":"220","author":"Chiu","year":"2024","journal-title":"Free Radic. Biol. Med."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"2304","DOI":"10.3390\/md9112304","article-title":"Antioxidant effect of a marine oligopeptide preparation from chum salmon (Oncorhynchus keta) by enzymatic hydrolysis in radiation injured mice","volume":"9","author":"Yang","year":"2011","journal-title":"Mar. Drugs"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1016\/S0955-2863(00)00110-8","article-title":"Identification of an Antihypertensive Peptide from Peptic Digest of Wakame (Undaria pinnatifida)","volume":"11","author":"Suetsuna","year":"2000","journal-title":"J. Nutr. Biochem."},{"key":"ref_145","doi-asserted-by":"crossref","unstructured":"Zheng, Y., Zhang, Y., and San, S. (2020). Efficacy of a Novel ACE-Inhibitory Peptide from Sargassum maclurei in Hypertension and Reduction of Intracellular Endothelin-1. Nutrients, 12.","DOI":"10.3390\/nu12030653"},{"key":"ref_146","doi-asserted-by":"crossref","unstructured":"Abachi, S., Bazinet, L., and Beaulieu, L. (2019). Antihypertensive and Angiotensin-I-Converting Enzyme (ACE)-Inhibitory Peptides from Fish as Potential Cardioprotective Compounds. Mar. Drugs, 17.","DOI":"10.3390\/md17110613"},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1038\/sj.jhh.1001065","article-title":"Antihypertensive effect of valyl-tyrosine, a short chain peptide derived from sardine muscle hydrolyzate, on mild hypertensive subjects","volume":"14","author":"Kawasaki","year":"2000","journal-title":"J. Hum. Hypertens."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"1541","DOI":"10.1271\/bbb.56.1541","article-title":"Peptide inhibitors for angiotensin i-converting enzyme from thermolysin digest of dried bonitot","volume":"56","author":"Yokoyama","year":"1992","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/S0162-3109(99)00118-6","article-title":"LKPNM: A prodrug-type ACE-inhibitory peptide derived from fish protein","volume":"44","author":"Fujita","year":"1999","journal-title":"Immunopharmacology"},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1002\/bab.1478","article-title":"Two novel peptides with angiotensin I converting enzyme inhibitory and antioxidative activities from Scorpaena notata muscle protein hydrolysate","volume":"64","author":"Aissaoui","year":"2017","journal-title":"Biotechnol. Appl. Biochem."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"6245","DOI":"10.1021\/jf020482t","article-title":"Angiotensin I-converting enzyme inhibitory peptides derived from wakame (Undaria pinnatifida) and their antihypertensive effect in spontaneously hypertensive rats","volume":"50","author":"Sato","year":"2002","journal-title":"J. Agric. Food Chem."},{"key":"ref_152","doi-asserted-by":"crossref","unstructured":"Cao, J., Xiang, B., Dou, B., Hu, J., Zhang, L., Kang, X., Lyu, M., and Wang, S. (2024). Novel Angiotensin-Converting Enzyme-Inhibitory Peptides Obtained from Trichiurus lepturus: Preparation, Identification and Potential Antihypertensive Mechanism. Biomolecules, 14.","DOI":"10.3390\/biom14050581"},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"119","DOI":"10.3390\/md403119","article-title":"Conotoxins: Therapeutic Potential and Application","volume":"4","author":"Layer","year":"2006","journal-title":"Mar. Drugs"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/S0304-3959(01)00436-5","article-title":"The novel N-type calcium channel blocker, AM336, produces potent dose-dependent antinociception after intrathecal dosing in rats and inhibits substance P release in rat spinal cord slices","volume":"96","author":"Smith","year":"2002","journal-title":"Pain"},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"790","DOI":"10.1038\/nrd1197","article-title":"Therapeutic potential of venom peptides","volume":"2","author":"Lewis","year":"2003","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_156","doi-asserted-by":"crossref","unstructured":"Herzig, V., Cristofori-Armstrong, B., Israel, M.R., Nixon, S.A., Vetter, I., and King, G.F. (2020). Animal toxins\u2014Nature\u2019s evolutionary-refined toolkit for basic research and drug discovery. Biochem. Pharmacol., 181.","DOI":"10.1016\/j.bcp.2020.114096"},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"1546","DOI":"10.2174\/156802612802652457","article-title":"Therapeutic potential of cone snail venom peptides (conopeptides)","volume":"12","author":"Vetter","year":"2012","journal-title":"Curr. Top. Med. Chem."},{"key":"ref_158","doi-asserted-by":"crossref","unstructured":"Robinson, S.D., and Vetter, I. (2020). Pharmacology and therapeutic potential of venom peptides. Biochem. Pharmacol., 181.","DOI":"10.1016\/j.bcp.2020.114207"},{"key":"ref_159","doi-asserted-by":"crossref","unstructured":"Cardoso, R.R., Sarandy, M.M., de Oliveira, L.L., da Matta, S.L.P., Novaes, R.D., and Gon\u00e7alves, R.V. (2024). Positive Effect of Peptides Obtained from Nile Tilapia (Oreochromis niloticus) on Inflammation Regulation and Wound Healing. Cosmetics, 11.","DOI":"10.3390\/cosmetics11040133"},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"4247","DOI":"10.29219\/fnr.v64.4247","article-title":"Marine fish peptides (collagen peptides) compound intake promotes wound healing in rats after cesarean section","volume":"64","author":"Peng","year":"2020","journal-title":"Food Nutr. Res."},{"key":"ref_161","first-page":"44","article-title":"Clinical innovation: Fish-derived wound product for cutaneous wounds","volume":"9","author":"Sitje","year":"2018","journal-title":"Wounds Int."},{"key":"ref_162","doi-asserted-by":"crossref","unstructured":"Rey-Campos, M., Moreira, R., Romero, A., Medina-Gali, R.M., Novoa, B., Gasset, M., and Figueras, A. (2020). Transcriptomic Analysis Reveals the Wound Healing Activity of Mussel Myticin, C. Biomolecules, 10.","DOI":"10.3390\/biom10010133"},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"1296","DOI":"10.1128\/AAC.00948-10","article-title":"Therapeutic efficacy of halocidin-derived peptide HG1 in a mouse model of surgical wound infection with methicillin-resistant Staphylococcus aureus","volume":"55","author":"Lee","year":"2011","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_164","doi-asserted-by":"crossref","unstructured":"Yang, H., Zhang, Q., Zhang, B., Zhao, Y., and Wang, N. (2023). Potential Active Marine Peptides as Anti-Aging Drugs or Drug Candidates. Mar. Drugs, 21.","DOI":"10.3390\/md21030144"},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1007\/978-981-13-3681-2_13","article-title":"Health benefits of anti-aging drugs","volume":"91","author":"Piskovatska","year":"2019","journal-title":"Biochem. Cell Biol. Ageing Part II Clin. Sci."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"103954","DOI":"10.1016\/j.jff.2020.103954","article-title":"Preparation of sea cucumber (Stichopus variegates) peptide fraction with desired organoleptic property and its anti-aging activity in fruit flies and D-galactose-induced aging mice","volume":"69","author":"Lin","year":"2020","journal-title":"J. Funct. Foods"},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"5004","DOI":"10.1039\/D0FO00560F","article-title":"Antioxidant and anti-aging effects of a sea cucumber protein hydrolyzate and bioinformatic characterization of its composing peptides","volume":"11","author":"Guo","year":"2020","journal-title":"Food Funct."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.jff.2018.05.033","article-title":"Anti-aging effect of sea cucumber (Cucumaria frondosa) hydrolysate on fruit flies and d-galactose-induced aging mice","volume":"47","author":"Lin","year":"2018","journal-title":"J. Funct. Foods"},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/j.neurobiolaging.2013.07.019","article-title":"Klotho upregulation contributes to the neuroprotection of ligustilide in an Alzheimer\u2019s disease mouse model","volume":"35","author":"Kuang","year":"2014","journal-title":"Neurobiol. Aging"},{"key":"ref_170","doi-asserted-by":"crossref","unstructured":"Alvari\u00f1o, R., Alonso, E., Bornancin, L., Bonnard, I., Inguimbert, N., Banaigs, B., and Botana, L.M. (2020). Biological Activities of Cyclic and Acyclic B-Type Laxaphycins in SH-SY5Y Human Neuroblastoma Cells. Mar. Drugs, 18.","DOI":"10.3390\/md18070364"},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"104677","DOI":"10.1016\/j.jff.2021.104677","article-title":"High-degree hydrolysis sea cucumber peptides improve exercise performance and exert antifatigue effect via activating the NRF2 and AMPK signaling pathways in mice","volume":"86","author":"Wang","year":"2021","journal-title":"J. Funct. Foods"},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.foodchem.2020.127094","article-title":"The novel peptides ICRD and LCGEC screened from tuna roe show antioxidative activity via Keap1\/Nrf2-ARE pathway regulation and gut microbiota modulation","volume":"327","author":"Han","year":"2020","journal-title":"Food Chem."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"3508","DOI":"10.29219\/fnr.v63.3508","article-title":"Antiphotoaging effect of boiled abalone residual peptide ATPGDEG on UVB-induced keratinocyte HaCaT cells","volume":"63","author":"Chen","year":"2019","journal-title":"Food Nutr. Res."},{"key":"ref_174","doi-asserted-by":"crossref","unstructured":"Cai, W.-W., Hu, X.-M., Wang, Y.-M., Chi, C.-F., and Wang, B. (2022). Bioactive Peptides from Skipjack Tuna Cardiac Arterial Bulbs: Preparation, Identification, Antioxidant Activity, and Stability against Thermal, pH, and Simulated Gastrointestinal Digestion Treatments. Mar. Drugs, 20.","DOI":"10.3390\/md20100626"},{"key":"ref_175","doi-asserted-by":"crossref","unstructured":"Pan, N., Li, Z.-C., Li, Z.-H., Chen, S.-H., Jiang, M.-H., Yang, H.-Y., Liu, Y.-S., Hu, R., Zeng, Y.-W., and Dai, L.-H. (2022). Antiplatelet and Antithrombotic Effects of Isaridin E Isolated from the Marine-Derived Fungus via Downregulating the PI3K\/Akt Signaling Pathway. Mar. Drugs, 20.","DOI":"10.3390\/md20010023"},{"key":"ref_176","doi-asserted-by":"crossref","unstructured":"Battistuzzi, F.U., Feijao, A., and Hedges, S.B. (2004). A genomic timescale of prokaryote evolution: Insights into the origin of methanogenesis, phototrophy, and the colonization of land. BMC Evol. Biol., 4.","DOI":"10.1186\/1471-2148-4-44"},{"key":"ref_177","doi-asserted-by":"crossref","unstructured":"Guryanova, S.V. (2023). Immunomodulation, Bioavailability and Safety of Bacteriocins. Life, 13.","DOI":"10.3390\/life13071521"},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"13624","DOI":"10.1073\/pnas.1110633108","article-title":"Estimating the timing of early eukaryotic diversification with multigene molecular clocks","volume":"108","author":"Parfrey","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1038\/mi.2013.37","article-title":"Pleurocidin, a novel antimicrobial peptide, induces human mast cell activation through the FPRL1 receptor","volume":"7","author":"Pundir","year":"2014","journal-title":"Mucosal Immunol."},{"key":"ref_180","first-page":"76","article-title":"A Pleurocidin-Like Peptide from Poecilia Mexicana Fish Induces Selective Cytotoxicity in Leukemia Jurkat Cells Through the Apoptosis Pathway","volume":"25","author":"Ebrahimdoost","year":"2023","journal-title":"Cell"},{"key":"ref_181","first-page":"195","article-title":"Aquatic peptides: Prospects and limitations in developing them as therapeutic products","volume":"15","author":"Velayutham","year":"2022","journal-title":"AACL Bioflux"},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"4006","DOI":"10.3390\/md13074006","article-title":"Marine Peptides: Bioactivities and Applications","volume":"13","author":"Cheung","year":"2015","journal-title":"Mar. Drugs"},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"1475","DOI":"10.4155\/fmc.11.118","article-title":"Marine natural products: A new wave of drugs?","volume":"3","author":"Montaser","year":"2011","journal-title":"Future Med. Chem."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.jchromb.2003.11.005","article-title":"Bioactive peptides from marine sources: Pharmacological properties and isolation procedures","volume":"803","author":"Aneiros","year":"2004","journal-title":"J. Chromatogr. B Analyt. Technol. Biomed. Life Sci."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"1336","DOI":"10.1021\/np020184q","article-title":"Tasiamide, a cytotoxic peptide from the marine cyanobacterium Symploca sp.","volume":"65","author":"Williams","year":"2002","journal-title":"J. Nat. Prod."},{"key":"ref_186","doi-asserted-by":"crossref","unstructured":"Kanaujia, K.A., Wagh, S., Pandey, G., Phatale, V., Khairnar, P., Kolipaka, T., Rajinikanth, P.S., Saraf, S.A., Srivastava, S., and Kumar, S. (2025). Harnessing marine antimicrobial peptides for novel therapeutics: A deep dive into ocean-derived bioactives. Int. J. Biol. Macromol., 307.","DOI":"10.1016\/j.ijbiomac.2025.142158"},{"key":"ref_187","doi-asserted-by":"crossref","unstructured":"Wang, J., Li, F., Li, W., Li, Y., Zhang, J., and Qin, S. (2025). Progress in Preparation Technology and Functional Research on Marine Bioactive Peptides. Mar. Biotechnol., 27.","DOI":"10.1007\/s10126-024-10401-0"},{"key":"ref_188","doi-asserted-by":"crossref","unstructured":"Qiao, K., Huang, Q., Sun, T., Chen, B., Huang, W., Su, Y., Lin, H., and Liu, Z. (2024). Preparation and Efficacy Evaluation of Antihyperuricemic Peptides from Marine Sources. Nutrients, 16.","DOI":"10.3390\/nu16244301"},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"32","DOI":"10.12688\/f1000research.5984.2","article-title":"Enhancement of COPD biological networks using a web-based collaboration interface","volume":"4","author":"Hoeng","year":"2015","journal-title":"F1000 Res."},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1007\/978-1-4939-7027-8_2","article-title":"sbv IMPROVER: Modern Approach to Systems Biology","volume":"1613","author":"Guryanova","year":"2017","journal-title":"Methods Mol. Biol."},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"115308","DOI":"10.1016\/j.foodres.2024.115308","article-title":"Identification and anticoagulant mechanisms of novel factor XIa inhibitory peptides by virtual screening of a in silico generated deep-sea peptide database","volume":"197","author":"Ouyang","year":"2024","journal-title":"Food Res. Int."},{"key":"ref_192","doi-asserted-by":"crossref","unstructured":"Lee, A.C.-L., Harris, J.L., Khanna, K.K., and Hong, J.-H. (2019). A Comprehensive Review on Current Advances in Peptide Drug Development and Design. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20102383"},{"key":"ref_193","doi-asserted-by":"crossref","unstructured":"Rahman, A., Rehmani, R., Pirvu, D.G., Huang, S.M., Puri, S., and Arcos, M. (2024). Unlocking the Therapeutic Potential of Marine Collagen: A Scientific Exploration for Delaying Skin Aging. Mar. Drugs, 22.","DOI":"10.20944\/preprints202401.1842.v1"},{"key":"ref_194","doi-asserted-by":"crossref","unstructured":"Geahchan, S., Baharlouei, P., and Rahman, A. (2022). Marine Collagen: A Promising Biomaterial for Wound Healing, Skin Anti-Aging, and Bone Regeneration. Mar. Drugs, 20.","DOI":"10.3390\/md20010061"},{"key":"ref_195","doi-asserted-by":"crossref","unstructured":"Salvatore, L., Gallo, N., Natali, M.L., Campa, L., Lunetti, P., Madaghiele, M., Blasi, F.S., Corallo, A., Capobianco, L., and Sannino, A. (2020). Marine collagen and its derivatives: Versatile and sustainable bio-resources for healthcare. Mater. Sci. Eng. C Mater. Biol. Appl., 113.","DOI":"10.1016\/j.msec.2020.110963"},{"key":"ref_196","doi-asserted-by":"crossref","unstructured":"Thiyagarasaiyar, K., Goh, B.-H., Jeon, Y.-J., and Yow, Y.-Y. (2020). Algae Metabolites in Cosmeceutical: An Overview of Current Applications and Challenges. Mar. Drugs, 18.","DOI":"10.3390\/md18060323"},{"key":"ref_197","doi-asserted-by":"crossref","unstructured":"Bauer, M., Glowacka, M., Kamysz, W., and Kleczkowska, P. (2024). Marine Peptides: Potential Basic Structures for the Development of Hybrid Compounds as Multitarget Therapeutics for the Treatment of Multifactorial Diseases. Int. J. Mol. Sci., 25.","DOI":"10.3390\/ijms252312601"},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"110365","DOI":"10.1016\/j.fsi.2025.110365","article-title":"Structure, function, and therapeutic potential of defensins from marine animals","volume":"163","author":"Lei","year":"2025","journal-title":"Fish Shellfish Immunol."},{"key":"ref_199","doi-asserted-by":"crossref","unstructured":"Yang, G., Lin, M., Kaliaperumal, K., Lu, Y., Qi, X., Jiang, X., Xu, X., Gao, C., Liu, Y., and Luo, X. (2024). Recent Advances in Anti-Inflammatory Compounds from Marine Microorganisms. Mar. Drugs, 22.","DOI":"10.3390\/md22090424"},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"445","DOI":"10.2174\/1574892813666180430110033","article-title":"Recent Progress of Marine Polypeptides as Anticancer Agents","volume":"13","author":"Zheng","year":"2018","journal-title":"Recent Pat. Anti-Cancer Drug Discov."},{"key":"ref_201","doi-asserted-by":"crossref","unstructured":"Baindara, P., Dinata, R., and Mandal, S.M. (2024). Marine Bacteriocins: An Evolutionary Gold Mine to Payoff Antibiotic Resistance. Mar. Drugs, 22.","DOI":"10.20944\/preprints202408.0442.v1"},{"key":"ref_202","doi-asserted-by":"crossref","unstructured":"Li, C.Q., Ma, Q.Y., Gao, X.Z., Wang, X., and Zhang, B.L. (2021). Research progress in anti-inflammatory bioactive substances derived from marine microorganisms, sponges, algae, and corals. Mar. Drugs, 19.","DOI":"10.3390\/md19100572"},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"e2300472","DOI":"10.1002\/advs.202300472","article-title":"Antimicrobial Peptide Synergies for Fighting Infectious Diseases","volume":"10","author":"Mhlongo","year":"2023","journal-title":"Adv. Sci."},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1080\/10826068.2024.2365357","article-title":"Antimicrobial peptides (AMPs) from microalgae as an alternative to conventional antibiotics in aquaculture","volume":"55","author":"Merlano","year":"2025","journal-title":"Prep. Biochem. Biotechnol."}],"container-title":["Marine Drugs"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1660-3397\/23\/7\/288\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,9]],"date-time":"2025-10-09T18:09:58Z","timestamp":1760033398000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1660-3397\/23\/7\/288"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,7,15]]},"references-count":204,"journal-issue":{"issue":"7","published-online":{"date-parts":[[2025,7]]}},"alternative-id":["md23070288"],"URL":"https:\/\/doi.org\/10.3390\/md23070288","relation":{},"ISSN":["1660-3397"],"issn-type":[{"value":"1660-3397","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,7,15]]}}}