{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,27]],"date-time":"2026-05-27T17:53:26Z","timestamp":1779904406593,"version":"3.53.1"},"reference-count":83,"publisher":"MDPI AG","issue":"8","license":[{"start":{"date-parts":[[2025,8,17]],"date-time":"2025-08-17T00:00:00Z","timestamp":1755388800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["32303034"],"award-info":[{"award-number":["32303034"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Marine Science Young Scientists Cultivation Program of the Guangxi Beibu Gulf Marine Science and Technology Innovation Cooperation Base","award":["24-03190010"],"award-info":[{"award-number":["24-03190010"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Marine Drugs"],"abstract":"<jats:p>The growing problem of antimicrobial resistance in aquaculture, caused by the excessive and unregulated use of antibiotics, highlights the critical necessity for developing new anti-infective solutions. Based on the characteristics of glycine-rich antimicrobial peptides (AMPs) and transcriptomic data, an antimicrobial peptide, namely AfRgly1, was discovered in this study. Subsequently, the peptide was obtained through heterologous expression in E. coli, and its antibacterial spectrum was determined. Molecular dynamics simulation and molecular biology experiments were conducted to explore the antibacterial target of AfRgly1. Results showed that the mRNA expression level of AfRgly1 was significantly upregulated after Vibrio alginolyticus infection. AfRgly1 has broad-spectrum antibacterial activity targeting on bacterial cell membrane, and it may also interact with bacterial DNA. AfRgly1 displayed low selectivity for fish red blood cells. These results indicate that AfRgly1 is an antimicrobial peptide with considerable potential for application in the development of therapeutic agents.<\/jats:p>","DOI":"10.3390\/md23080330","type":"journal-article","created":{"date-parts":[[2025,8,18]],"date-time":"2025-08-18T13:28:22Z","timestamp":1755523702000},"page":"330","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Heterologous Expression and Antimicrobial Targets of a Novel Glycine-Rich Antimicrobial Peptide from Artemia franciscana"],"prefix":"10.3390","volume":"23","author":[{"given":"Ming","family":"Tao","sequence":"first","affiliation":[{"name":"Biosafety Level 3 Laboratory of Shenzhen University, Shenzhen 518060, China"},{"name":"College of Life Sciences and Oceanography, Shenzhen University, Shenzhen 518060, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aobo","family":"Sun","sequence":"additional","affiliation":[{"name":"College of Life Sciences and Oceanography, Shenzhen University, Shenzhen 518060, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Huishi","family":"Shao","sequence":"additional","affiliation":[{"name":"College of Life Sciences and Oceanography, Shenzhen University, Shenzhen 518060, China"},{"name":"College of Marine Science BGU, Beibu Gulf University, Qinzhou 535011, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Huaiyuan","family":"Ye","sequence":"additional","affiliation":[{"name":"College of Life Sciences and Oceanography, Shenzhen University, Shenzhen 518060, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Guangming","family":"Yu","sequence":"additional","affiliation":[{"name":"College of Life Sciences and Oceanography, Shenzhen University, Shenzhen 518060, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daigeng","family":"Chen","sequence":"additional","affiliation":[{"name":"College of Marine Science BGU, Beibu Gulf University, Qinzhou 535011, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4135-998X","authenticated-orcid":false,"given":"Wei","family":"Zhang","sequence":"additional","affiliation":[{"name":"College of Life Sciences and Oceanography, Shenzhen University, Shenzhen 518060, China"},{"name":"College of Marine Science BGU, Beibu Gulf University, Qinzhou 535011, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,8,17]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1007\/s12571-021-01246-9","article-title":"The Contribution of Fisheries and Aquaculture to the Global Protein Supply","volume":"14","author":"Boyd","year":"2022","journal-title":"Food Secur."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1286","DOI":"10.1111\/raq.12897","article-title":"Impact of Bacteriocins on Multidrug-Resistant Bacteria and Their Application in Aquaculture Disease Prevention and Control","volume":"16","author":"Chen","year":"2024","journal-title":"Rev. Aquac."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"11786302241299368","DOI":"10.1177\/11786302241299369","article-title":"Multidrug-Resistant Bacteria in Aquaculture Systems in Accra, Ghana","volume":"18","author":"Dayie","year":"2024","journal-title":"Environ. Health Insights"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1039\/D3NP00031A","article-title":"Embracing the Era of Antimicrobial Peptides with Marine Organisms","volume":"41","author":"Chen","year":"2024","journal-title":"Nat. Prod. Rep."},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Bulet, P., Charlet, M., and Hetru, C. (2003). Antimicrobial Peptides in Insect Immunity. Innate Immunity, Springer.","DOI":"10.1007\/978-1-59259-320-0_5"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1016\/j.tips.2019.04.012","article-title":"The Vast Structural Diversity of Antimicrobial Peptides","volume":"40","author":"Koehbach","year":"2019","journal-title":"Trends Pharmacol. Sci."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"2287","DOI":"10.1007\/s00726-014-1820-1","article-title":"Proline-Rich Antimicrobial Peptides: Potential Therapeutics against Antibiotic-Resistant Bacteria","volume":"46","author":"Li","year":"2014","journal-title":"Amino Acids"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"781","DOI":"10.1016\/S0145-305X(03)00058-2","article-title":"Acanthoscurrin: A Novel Glycine-Rich Antimicrobial Peptide Constitutively Expressed in the Hemocytes of the Spider Acanthoscurria Gomesiana","volume":"27","author":"Lorenzini","year":"2003","journal-title":"Dev. Comp. Immunol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"1004","DOI":"10.1016\/j.bbamem.2012.11.017","article-title":"Selective Antimicrobial Activity and Mode of Action of Adepantins, Glycine-Rich Peptide Antibiotics Based on Anuran Antimicrobial Peptide Sequences","volume":"1828","author":"Guida","year":"2013","journal-title":"Biochim. Et Biophys. Acta (BBA) Biomembr."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"2604","DOI":"10.1016\/j.molimm.2009.05.002","article-title":"Glycine-Rich Multi-Domain Antimicrobial Peptide Isolated from the Spider Crab (Hyas Araneus) Hemocytes","volume":"46","author":"Sperstad","year":"2009","journal-title":"Mol. Immunol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1080\/10242422.2022.2124111","article-title":"Discussing the Roles of Proline and Glycine from the Perspective of Cold Adaptation in Lipases and Cellulases","volume":"41","author":"Atak","year":"2023","journal-title":"Biocatal. Biotransformation"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"2924","DOI":"10.1021\/acs.jmedchem.7b01831","article-title":"Antibacterial Activity Affected by the Conformational Flexibility in Glycine\u2013Lysine Based \u03b1-Helical Antimicrobial Peptides","volume":"61","author":"Krce","year":"2018","journal-title":"J. Med. Chem."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1385\/ABAB:120:3:169","article-title":"Glycine-Rich Proteins","volume":"120","author":"Mousavi","year":"2005","journal-title":"Appl. Biochem. Biotechnol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.toxicon.2009.03.011","article-title":"Leptoglycin: A New Glycine\/Leucine-Rich Antimicrobial Peptide Isolated from the Skin Secretion of the South American Frog Leptodactylus Pentadactylus (Leptodactylidae)","volume":"54","author":"Sousa","year":"2009","journal-title":"Toxicon"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"2945","DOI":"10.1007\/s10989-021-10302-z","article-title":"His-Rich Peptides, Gly- and His-Rich Peptides: Functionally Versatile Compounds with Potential Multi-Purpose Applications","volume":"27","author":"Nunes","year":"2021","journal-title":"Int. J. Pept. Res. Ther."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1049","DOI":"10.1248\/bpb.18.1049","article-title":"Purification and CDNA Cloning of an Antifungal Protein from the Hemolymph of Holotrichia Diomphalia Larvae","volume":"18","author":"Lee","year":"1995","journal-title":"Biol. Pharm. Bull."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"231","DOI":"10.3354\/dao053231","article-title":"Virulence of Luminous Vibrios to Artemia Franciscana Nauplii","volume":"53","author":"Roque","year":"2003","journal-title":"Dis. Aquat. Organ."},{"key":"ref_18","doi-asserted-by":"crossref","unstructured":"Saucedo-V\u00e1zquez, J.P., Gushque, F., Vispo, N.S., Rodriguez, J., Gudi\u00f1o-Gomezjurado, M.E., Albericio, F., Tellkamp, M.P., and Alexis, F. (2022). Marine Arthropods as a Source of Antimicrobial Peptides. Mar. Drugs, 20.","DOI":"10.3390\/md20080501"},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Brady, D., Grapputo, A., Romoli, O., and Sandrelli, F. (2019). Insect Cecropins, Antimicrobial Peptides with Potential Therapeutic Applications. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20235862"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/0304-4157(90)90006-X","article-title":"The Actions of Melittin on Membranes","volume":"1031","author":"Dempsey","year":"1990","journal-title":"Biochim. Et Biophys. Acta (BBA) Rev. Biomembr."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"758","DOI":"10.1016\/j.dci.2007.12.002","article-title":"Crustins: Enigmatic WAP Domain-Containing Antibacterial Proteins from Crustaceans","volume":"32","author":"Smith","year":"2008","journal-title":"Dev. Comp. Immunol."},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Bett, V.K., Macon, A., Vicoso, B., and Elkrewi, M. (2024). Chromosome-Level Assembly of Artemia Franciscana Sheds Light on Sex Chromosome Differentiation. Genome Biol. Evol., 16.","DOI":"10.1093\/gbe\/evae006"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1451","DOI":"10.1007\/s10989-019-09946-9","article-title":"Antimicrobial Peptides (AMPs): Roles, Functions and Mechanism of Action","volume":"26","author":"Seyfi","year":"2020","journal-title":"Int. J. Pept. Res. Ther."},{"key":"ref_24","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":"ref_25","doi-asserted-by":"crossref","first-page":"f1493","DOI":"10.1136\/bmj.f1493","article-title":"The True Cost of Antimicrobial Resistance","volume":"346","author":"Smith","year":"2013","journal-title":"BMJ Br. Med. J."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"4713","DOI":"10.2147\/IDR.S290835","article-title":"Antimicrobial Stewardship: Fighting Antimicrobial Resistance and Protecting Global Public Health","volume":"13","author":"Majumder","year":"2020","journal-title":"Infect. Drug Resist."},{"key":"ref_27","doi-asserted-by":"crossref","unstructured":"Luo, Y., and Song, Y. (2021). Mechanism of Antimicrobial Peptides: Antimicrobial, Anti-Inflammatory and Antibiofilm Activities. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms222111401"},{"key":"ref_28","first-page":"235","article-title":"Antimicrobial Peptides, An Alternative Antimicrobial Agent Against Multi-Drug-Resistant Microbes: Source, Application, and Potential","volume":"165","author":"Ramzah","year":"2023","journal-title":"Adv. Mater. Sci. Technol. Led Women"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1007\/s00343-012-1195-7","article-title":"Expression Profiles of Antimicrobial Peptides (AMPs) and Their Regulation by Relish","volume":"30","author":"Wang","year":"2012","journal-title":"Chin. J. Oceanol. Limnol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"1085","DOI":"10.1016\/j.molimm.2007.07.031","article-title":"Molecular Cloning, Genomic Organization and Recombinant Expression of a Crustin-like Antimicrobial Peptide from Black Tiger Shrimp Penaeus Monodon","volume":"45","author":"Amparyup","year":"2008","journal-title":"Mol. Immunol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"D285","DOI":"10.1093\/nar\/gky1030","article-title":"DbAMP: An Integrated Resource for Exploring Antimicrobial Peptides with Functional Activities and Physicochemical Properties on Transcriptome and Proteome Data","volume":"47","author":"Jhong","year":"2019","journal-title":"Nucleic Acids Res."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"711","DOI":"10.3390\/ph8040711","article-title":"Antimicrobial Peptides from Plants","volume":"8","author":"Tam","year":"2015","journal-title":"Pharmaceuticals"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"R14","DOI":"10.1016\/j.cub.2015.11.017","article-title":"Antimicrobial Peptides","volume":"26","author":"Zhang","year":"2016","journal-title":"Curr. Biol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1186\/s13568-016-0315-8","article-title":"Glycin-Rich Antimicrobial Peptide YD1 from B. Amyloliquefaciens, Induced Morphological Alteration in and Showed Affinity for Plasmid DNA of E. Coli","volume":"7","author":"Rahman","year":"2017","journal-title":"AMB Express"},{"key":"ref_35","doi-asserted-by":"crossref","unstructured":"He, Z., Fei, Z., Shi, H., Huang, M., Wei, L., Wang, J., He, P., and Zhang, W. (2025). Heterologous Expression and Antimicrobial Mechanism of a Cysteine-Rich Peptide from Barnacle Pollicipes Pollicipes. Microorganisms, 13.","DOI":"10.3390\/microorganisms13061381"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"1517","DOI":"10.1007\/s00299-023-03044-3","article-title":"Evolution of Antimicrobial Cysteine-Rich Peptides in Plants","volume":"42","author":"Ma","year":"2023","journal-title":"Plant Cell Rep."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"107173","DOI":"10.1016\/j.toxicon.2023.107173","article-title":"Cysteine-Rich Peptides: From Bioactivity to Bioinsecticide Applications","volume":"230","author":"Ho","year":"2023","journal-title":"Toxicon"},{"key":"ref_38","doi-asserted-by":"crossref","unstructured":"Holzknecht, J., and Marx, F. (2024). Navigating the Fungal Battlefield: Cysteine-Rich Antifungal Proteins and Peptides from Eurotiales. Front. Fungal Biol., 5.","DOI":"10.3389\/ffunb.2024.1451455"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"135","DOI":"10.4149\/gpb_2015002","article-title":"Interaction of Cysteine-Rich Cationic Antimicrobial Peptides with Intact Bacteria and Model Membranes","volume":"34","author":"Nagy","year":"2015","journal-title":"Gen. Physiol. Biophys."},{"key":"ref_40","doi-asserted-by":"crossref","unstructured":"Lai, Z., Yuan, X., Chen, H., Zhu, Y., Dong, N., and Shan, A. (2022). Strategies Employed in the Design of Antimicrobial Peptides with Enhanced Proteolytic Stability. Biotechnol. Adv., 59.","DOI":"10.1016\/j.biotechadv.2022.107962"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1128\/MMBR.67.4.593-656.2003","article-title":"Molecular Basis of Bacterial Outer Membrane Permeability Revisited","volume":"67","author":"Hiroshi","year":"2003","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"10378","DOI":"10.1074\/jbc.M412865200","article-title":"A Molecular Mechanism for Lipopolysaccharide Protection of Gram-Negative Bacteria from Antimicrobial Peptides*","volume":"280","author":"Papo","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"115377","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":"ref_44","doi-asserted-by":"crossref","first-page":"936","DOI":"10.1016\/j.bbamem.2015.11.004","article-title":"Gram-Positive Bacterial Cell Envelopes: The Impact on the Activity of Antimicrobial Peptides","volume":"1858","author":"Malanovic","year":"2016","journal-title":"Biochim. Et Biophys. Acta (BBA) Biomembr."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/0022-2836(82)90515-0","article-title":"A Simple Method for Displaying the Hydropathic Character of a Protein","volume":"157","author":"Kyte","year":"1982","journal-title":"J. Mol. Biol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"5390","DOI":"10.1021\/acsomega.8b00293","article-title":"Small Cationic Peptides: Influence of Charge on Their Antimicrobial Activity","volume":"3","author":"Zenak","year":"2018","journal-title":"ACS Omega"},{"key":"ref_47","first-page":"360","article-title":"Membrane Interactions of Designed Cationic Antimicrobial Peptides: The Two Thresholds","volume":"89","author":"Glukhov","year":"2008","journal-title":"Biopolym. Orig. Res. Biomol."},{"key":"ref_48","doi-asserted-by":"crossref","unstructured":"Zhang, W., Wei, L., Chen, P., Ning, B., Wang, J., He, P., Shang, C., and Yu, D. (2024). Discovery and Characterization of an Atypical Crustin Antimicrobial Peptide from Pollicipes Pollicipes. Mar. Drugs, 22.","DOI":"10.3390\/md22120526"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"4053","DOI":"10.1093\/nar\/gki725","article-title":"Structural and DNA-Binding Studies on the Bovine Antimicrobial Peptide, Indolicidin: Evidence for Multiple Conformations Involved in Binding to Membranes and DNA","volume":"33","author":"Hsu","year":"2005","journal-title":"Nucleic Acids Res."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"1173","DOI":"10.1002\/jps.20627","article-title":"In Vitro Hemolysis: Guidance for the Pharmaceutical Scientist","volume":"95","author":"Amin","year":"2006","journal-title":"J. Pharm. Sci."},{"key":"ref_51","first-page":"2202","article-title":"Peptide Signals Sense and Destroy Target Cells","volume":"306","author":"Garsin","year":"2004","journal-title":"Science (1979)"},{"key":"ref_52","doi-asserted-by":"crossref","unstructured":"Lumangtad, L.A., and Bell, T.W. (2020). The Signal Peptide as a New Target for Drug Design. Bioorganic Med. Chem. Lett., 30.","DOI":"10.1016\/j.bmcl.2020.127115"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1186\/s12934-019-1078-0","article-title":"The YoaW Signal Peptide Directs Efficient Secretion of Different Heterologous Proteins Fused to a StrepII-SUMO Tag in Bacillus Subtilis","volume":"18","author":"Heinrich","year":"2019","journal-title":"Microb. Cell Fact."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"1369","DOI":"10.1007\/s10295-015-1673-y","article-title":"Expression of Plectasin in Bacillus Subtilis Using SUMO Technology by a Maltose-Inducible Vector","volume":"42","author":"Zhang","year":"2015","journal-title":"J. Ind. Microbiol. Biotechnol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1007\/s10930-023-10144-2","article-title":"Soluble Expression of Antimicrobial Peptide BSN-37 from Escherichia Coli by SUMO Fusion Technology","volume":"42","author":"Xu","year":"2023","journal-title":"Protein J."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"7136","DOI":"10.1016\/j.vaccine.2011.05.073","article-title":"Cloning and Expression of Protease ClpP from Streptococcus Pneumoniae in Escherichia Coli: Study of the Influence of Kanamycin and IPTG Concentration on Cell Growth, Recombinant Protein Production and Plasmid Stability","volume":"29","author":"Einsfeldt","year":"2011","journal-title":"Vaccine"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1016\/j.pep.2011.08.001","article-title":"Recombinant Production of Antimicrobial Peptides in Escherichia Coli: A Review","volume":"80","author":"Li","year":"2011","journal-title":"Protein Expr. Purif."},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Kang, L., Weng, N., and Jian, W. (2020). LC\u2013MS Bioanalysis of Intact Proteins and Peptides. Biomed. Chromatogr., 34.","DOI":"10.1002\/bmc.4633"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"3568","DOI":"10.1021\/cr068213f","article-title":"Limitations and Pitfalls in Protein Identification by Mass Spectrometry","volume":"107","author":"Lubec","year":"2007","journal-title":"Chem. Rev."},{"key":"ref_60","doi-asserted-by":"crossref","unstructured":"Zhuang, H., Ou, Y., Chen, R., Huang, D., and Wang, C. (2023). Comparing the Ability of Secretory Signal Peptides for Heterologous Expression of Anti-Lipopolysaccharide Factor 3 in Chlamydomonas Reinhardtii. Mar. Drugs, 21.","DOI":"10.3390\/md21060346"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"100393","DOI":"10.1016\/j.aqrep.2020.100393","article-title":"Genome-Wide Screening of the Classical Cadherin Gene Family and Cadherin-1 Expression Response Infected with Streptococcus Agalactiae in Nile Tilapia (Oreochromis Niloticus)","volume":"17","author":"Yang","year":"2020","journal-title":"Aquac. Rep."},{"key":"ref_62","doi-asserted-by":"crossref","unstructured":"Yang, H., Li, S., Li, F., and Xiang, J. (2016). Structure and Bioactivity of a Modified Peptide Derived from the LPS-Binding Domain of an Anti-Lipopolysaccharide Factor (ALF) of Shrimp. Mar. Drugs, 14.","DOI":"10.3390\/md14050096"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"907","DOI":"10.1038\/s41587-019-0201-4","article-title":"Graph-Based Genome Alignment and Genotyping with HISAT2 and HISAT-Genotype","volume":"37","author":"Kim","year":"2019","journal-title":"Nat. Biotechnol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1650","DOI":"10.1038\/nprot.2016.095","article-title":"Transcript-Level Expression Analysis of RNA-Seq Experiments with HISAT, StringTie and Ballgown","volume":"11","author":"Pertea","year":"2016","journal-title":"Nat. Protoc. Erecipes Res."},{"key":"ref_65","doi-asserted-by":"crossref","unstructured":"Chen, Y., Lun, A.T.L., and Smyth, G.K. (2014). Differential Expression Analysis of Complex RNA-Seq Experiments Using EdgeR, Springer International Publishing.","DOI":"10.1007\/978-3-319-07212-8_3"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1038\/s41587-021-01156-3","article-title":"SignalP 6.0 Predicts All Five Types of Signal Peptides Using Protein Language Models","volume":"40","author":"Teufel","year":"2022","journal-title":"Nat. Biotechnol."},{"key":"ref_67","doi-asserted-by":"crossref","unstructured":"Horton, P., Park, K.-J., Obayashi, T., and Nakai, K. (2006, January 12\u201316). Protein Subcellular localization prediction with wolf psort. Proceedings of the 4th Asia-Pacific Bioinformatics Conference, Taipei, Taiwan.","DOI":"10.1142\/9781860947292_0007"},{"key":"ref_68","first-page":"7","article-title":"AlphaFold 3 to Offer Structure Prediction via Web Browser","volume":"102","author":"Oldach","year":"2024","journal-title":"Chem. Eng. News"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"D1094","DOI":"10.1093\/nar\/gkv1051","article-title":"CAMPR3: A Database on Sequences, Structures and Signatures of Antimicrobial Peptides","volume":"44","author":"Waghu","year":"2016","journal-title":"Nucleic Acids Res."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"3257","DOI":"10.1021\/ct300400x","article-title":"Optimization of the Additive CHARMM All-Atom Protein Force Field Targeting Improved Sampling of the Backbone \u03d5, \u03c8 and Side-Chain \u03a71 and \u03a72 Dihedral Angles","volume":"8","author":"Best","year":"2012","journal-title":"J. Chem. Theory Comput."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"1091","DOI":"10.1529\/biophysj.104.048835","article-title":"Phosphatidylethanolamine-Phosphatidylglycerol Bilayer as a Model of the Inner Bacterial Membrane","volume":"88","author":"Murzyn","year":"2005","journal-title":"Biophys. J."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1007\/s00894-018-3747-z","article-title":"A Coarse-Grained Approach to Studying the Interactions of the Antimicrobial Peptides Aurein 1.2 and Maculatin 1.1 with POPG\/POPE Lipid Mixtures","volume":"24","author":"Balatti","year":"2018","journal-title":"J. Mol. Model."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"3684","DOI":"10.1063\/1.448118","article-title":"Molecular Dynamics with Coupling to an External Bath","volume":"81","author":"Berendsen","year":"1984","journal-title":"J. Chem. Phys."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.softx.2015.06.001","article-title":"GROMACS: High Performance Molecular Simulations through Multi-Level Parallelism from Laptops to Supercomputers","volume":"1","author":"Abraham","year":"2015","journal-title":"SoftwareX"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/0263-7855(96)00018-5","article-title":"VMD: Visual Molecular Dynamics","volume":"14","author":"Humphrey","year":"1996","journal-title":"J. Mol. Graph."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"8577","DOI":"10.1063\/1.470117","article-title":"A Smooth Particle Mesh Ewald Method","volume":"103","author":"Essmann","year":"1995","journal-title":"J. Chem. Phys."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"10089","DOI":"10.1063\/1.464397","article-title":"An N\u22c5Log (N) Method for Ewald Sums in Large Systems","volume":"98","author":"Darden","year":"1993","journal-title":"J. Chem. Phys."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"014101","DOI":"10.1063\/1.2408420","article-title":"Canonical Sampling through Velocity Rescaling","volume":"126","author":"Bussi","year":"2007","journal-title":"J. Chem. Phys."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"114107","DOI":"10.1063\/5.0020514","article-title":"Pressure Control Using Stochastic Cell Rescaling","volume":"153","author":"Bernetti","year":"2020","journal-title":"J. Chem. Phys."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"1463","DOI":"10.1002\/(SICI)1096-987X(199709)18:12<1463::AID-JCC4>3.0.CO;2-H","article-title":"LINCS: A Linear Constraint Solver for Molecular Simulations","volume":"18","author":"Hess","year":"1997","journal-title":"J. Comput. Chem."},{"key":"ref_81","doi-asserted-by":"crossref","unstructured":"Zhang, W., Xu, X., Zhang, J., Ye, T., Zhou, Q., Xu, Y., Li, W., Hu, Z., and Shang, C. (2022). Discovery and Characterization of a New Crustin Antimicrobial Peptide from Amphibalanus Amphitrite. Pharmaceutics, 14.","DOI":"10.3390\/pharmaceutics14020413"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1128\/jb.135.1.153-160.1978","article-title":"Cellular Lysis of Streptococcus Faecalis Induced with Triton X-100","volume":"135","author":"Cornett","year":"1978","journal-title":"J. Bacteriol."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/S0378-1097(03)00791-2","article-title":"A Simple and Efficient Triton X-100 Boiling and Chloroform Extraction Method of RNA Isolation from Gram-Positive and Gram-Negative Bacteria","volume":"229","author":"Sung","year":"2003","journal-title":"FEMS Microbiol. Lett."}],"container-title":["Marine Drugs"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1660-3397\/23\/8\/330\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,16]],"date-time":"2025-10-16T07:34:20Z","timestamp":1760600060000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1660-3397\/23\/8\/330"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,8,17]]},"references-count":83,"journal-issue":{"issue":"8","published-online":{"date-parts":[[2025,8]]}},"alternative-id":["md23080330"],"URL":"https:\/\/doi.org\/10.3390\/md23080330","relation":{},"ISSN":["1660-3397"],"issn-type":[{"value":"1660-3397","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,8,17]]}}}