{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,11]],"date-time":"2026-09-11T04:06:33Z","timestamp":1789099593830,"version":"build-2803163510"},"reference-count":44,"publisher":"MDPI AG","issue":"5","license":[{"start":{"date-parts":[[2026,4,27]],"date-time":"2026-04-27T00:00:00Z","timestamp":1777248000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100006769","name":"Russian Science Foundation","doi-asserted-by":"publisher","award":["22-14-00380-P"],"award-info":[{"award-number":["22-14-00380-P"]}],"id":[{"id":"10.13039\/501100006769","id-type":"DOI","asserted-by":"publisher"}]},{"award":["22-14-00380-P"],"award-info":[{"award-number":["22-14-00380-P"]}],"id":[{"id":"https:\/\/ror.org\/03y2gwe85","id-type":"ROR","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Marine Drugs"],"abstract":"<jats:p>The rise in antimicrobial resistance represents a significant challenge to global health. The reason partially lies in an inappropriate use of conventional antibiotics and the subsequent rapid spread of multidrug-resistant pathogen strains. This emergency requires an urgent search for conceptually new antimicrobial agents. A viable alternative to conventional antibiotics is antimicrobial peptides (AMPs), which are ribosomally synthesized molecules with considerable potential as next-generation anti-infectious therapeutics. Previously, we have reported on the \u03b2-hairpin peptide Ap9, an analog of abarenicin from the marine polychaeta Abarenicola pacifica, with potent activity against key Gram-negative pathogens. Here, it is shown that Ap9 acts in a manner resembling polymyxin B, namely via interaction with lipopolysaccharide (LPS), and retains its activity against polymyxin-resistant isolates without observed cross-resistance, and causes insignificant damage in cytoplasmic membrane at bactericidal concentrations. NMR spectroscopy reveals that LPS binding induces a conformational rearrangement of Ap9, its dimer formation, and local structural remodeling of the peptide region (residues 8\u201312) into 310-helix. Bacterial resistance to Ap9 was found to be relatively low with a reduced susceptibility associated with infrequent genetic alterations, such as the mutation in lptD or the deletion in mlaA. Furthermore, Ap9 demonstrates a favorable tolerability, a wider therapeutic window than that of polymyxin B, and a sufficiently long half-life through the systemic use, as well as in vivo efficacy in murine models of Gram-negative infections, including sepsis caused by the mcr-1-harboring Escherichia coli strain. The obtained results point to Ap9 as a promising candidate for further preclinical studies aimed at development of an alternative to polymyxins.<\/jats:p>","DOI":"10.3390\/md24050154","type":"journal-article","created":{"date-parts":[[2026,4,28]],"date-time":"2026-04-28T07:49:36Z","timestamp":1777362576000},"page":"154","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Marine Antimicrobial Peptide as a Promising Alternative to Polymyxin B"],"prefix":"10.3390","volume":"24","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2695-0157","authenticated-orcid":false,"given":"Victoria N.","family":"Safronova","sequence":"first","affiliation":[{"name":"M.M. Shemyakin & Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1788-1153","authenticated-orcid":false,"given":"Vladislav A.","family":"Lushpa","sequence":"additional","affiliation":[{"name":"M.M. Shemyakin & Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, Russia"},{"name":"Moscow Center for Advanced Studies, 123592 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6361-1042","authenticated-orcid":false,"given":"Victoria O.","family":"Shipunova","sequence":"additional","affiliation":[{"name":"M.M. Shemyakin & Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, Russia"},{"name":"Moscow Center for Advanced Studies, 123592 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0155-4414","authenticated-orcid":false,"given":"Marta V.","family":"Volovik","sequence":"additional","affiliation":[{"name":"Frumkin Institute of Physical Chemistry and Electrochemistry, Russian Academy of Sciences, 119071 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4778-344X","authenticated-orcid":false,"given":"Kira L.","family":"Dobrochaeva","sequence":"additional","affiliation":[{"name":"M.M. Shemyakin & Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Roman N.","family":"Kruglikov","sequence":"additional","affiliation":[{"name":"M.M. Shemyakin & Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3539-4906","authenticated-orcid":false,"given":"Ilia A.","family":"Bolosov","sequence":"additional","affiliation":[{"name":"M.M. Shemyakin & Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dmitrii E.","family":"Dashevskii","sequence":"additional","affiliation":[{"name":"Moscow Center for Advanced Studies, 123592 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3759-380X","authenticated-orcid":false,"given":"Alexey V.","family":"Mishin","sequence":"additional","affiliation":[{"name":"Moscow Center for Advanced Studies, 123592 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9581-2233","authenticated-orcid":false,"given":"Oleg V.","family":"Batishchev","sequence":"additional","affiliation":[{"name":"Frumkin Institute of Physical Chemistry and Electrochemistry, Russian Academy of Sciences, 119071 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Olga V.","family":"Korobova","sequence":"additional","affiliation":[{"name":"State Research Center for Applied Microbiology & Biotechnology, 142279 Obolensk, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6309-7645","authenticated-orcid":false,"given":"Alexander I.","family":"Borzilov","sequence":"additional","affiliation":[{"name":"State Research Center for Applied Microbiology & Biotechnology, 142279 Obolensk, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gulsara A.","family":"Slashcheva","sequence":"additional","affiliation":[{"name":"Branch of M.M. Shemyakin & Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 142290 Pushchino, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3053-2804","authenticated-orcid":false,"given":"Igor A.","family":"Dyachenko","sequence":"additional","affiliation":[{"name":"Branch of M.M. Shemyakin & Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 142290 Pushchino, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3635-1609","authenticated-orcid":false,"given":"Eduard V.","family":"Bocharov","sequence":"additional","affiliation":[{"name":"M.M. Shemyakin & Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, Russia"},{"name":"Moscow Center for Advanced Studies, 123592 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8448-031X","authenticated-orcid":false,"given":"Pavel V.","family":"Panteleev","sequence":"additional","affiliation":[{"name":"M.M. Shemyakin & Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, Russia"},{"name":"Moscow Center for Advanced Studies, 123592 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 & 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":[[2026,4,27]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"179124","DOI":"10.1016\/j.scitotenv.2025.179124","article-title":"Spread of Antimicrobial-Resistant Clones of the ESKAPEE Group: From the Clinical Setting to Hospital Effluent","volume":"973","author":"Krul","year":"2025","journal-title":"Sci. Total Environ."},{"key":"ref_2","unstructured":"WHO (2024). Bacterial Priority Pathogens List 2024: Bacterial Pathogens of Public Health Importance, to Guide Research, Development, and Strategies to Prevent and Control Antimicrobial Resistance, World Health Organization. [1st ed.]."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"e02097\u201322","DOI":"10.1128\/spectrum.02097-22","article-title":"Emergence and Transmission of Plasmid-Mediated Mobile Colistin Resistance Gene Mcr-10 in Humans and Companion Animals","volume":"10","author":"Yin","year":"2022","journal-title":"Microbiol. Spectr."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"102647","DOI":"10.1016\/j.sbi.2023.102647","article-title":"Structural Biology of MCR-1-Mediated Resistance to Polymyxin Antibiotics","volume":"82","author":"Materon","year":"2023","journal-title":"Curr. Opin. Struct. Biol."},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Shahzad, S., Willcox, M.D.P., and Rayamajhee, B. (2023). A Review of Resistance to Polymyxins and Evolving Mobile Colistin Resistance Gene (Mcr) among Pathogens of Clinical Significance. Antibiotics, 12.","DOI":"10.3390\/antibiotics12111597"},{"key":"ref_6","first-page":"55","article-title":"Mechanisms of Polymyxin Resistance","volume":"Volume 1145","author":"Li","year":"2019","journal-title":"Polymyxin Antibiotics: From Laboratory Bench to Bedside"},{"key":"ref_7","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_8","doi-asserted-by":"crossref","first-page":"3184","DOI":"10.1038\/s41467-020-16950-x","article-title":"An Amphipathic Peptide with Antibiotic Activity against Multidrug-Resistant Gram-Negative Bacteria","volume":"11","author":"Elliott","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"3392","DOI":"10.1038\/s41598-017-03664-2","article-title":"Antibacterial and Detoxifying Activity of NZ17074 Analogues with Multi-Layers of Selective Antimicrobial Actions against Escherichia coli and Salmonella enteritidis","volume":"7","author":"Yang","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1002\/psc.2732","article-title":"Design of Antimicrobial Peptide Arenicin Analogs with Improved Therapeutic Indices: Design of Arenicin Analogs with Improved Therapeutic Indices","volume":"21","author":"Panteleev","year":"2015","journal-title":"J. Pept. Sci."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1002\/bab.1456","article-title":"Improved Strategy for Recombinant Production and Purification of Antimicrobial Peptide Tachyplesin I and Its Analogs with High Cell Selectivity","volume":"64","author":"Panteleev","year":"2017","journal-title":"Biotech. App. Biochem."},{"key":"ref_12","unstructured":"Clinical and Laboratory Standards Institute (1999). Methods for Determining Bactericidal Activity of Antimicrobial Agents, CLSI."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"19003","DOI":"10.1021\/acs.langmuir.5c00963","article-title":"Dialectics of Antimicrobial Peptides II: Theoretical Models of Pore Formation and Membrane Protection","volume":"41","author":"Kondrashov","year":"2025","journal-title":"Langmuir"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"18986","DOI":"10.1021\/acs.langmuir.5c00962","article-title":"Dialectics of Antimicrobial Peptides I: Common Mechanisms of Offensive and Protecting Roles of the Peptides","volume":"41","author":"Volovik","year":"2025","journal-title":"Langmuir"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"3222","DOI":"10.1128\/AAC.47.10.3222-3232.2003","article-title":"Mutation Rate and Evolution of Fluoroquinolone Resistance in Escherichia coli Isolates from Patients with Urinary Tract Infections","volume":"47","author":"Karlsson","year":"2003","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"4538","DOI":"10.1038\/s41467-019-12364-6","article-title":"Integrated Evolutionary Analysis Reveals Antimicrobial Peptides with Limited Resistance","volume":"10","author":"Spohn","year":"2019","journal-title":"Nat. Commun."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1113","DOI":"10.1093\/nar\/23.7.1113","article-title":"Seryl-tRNA Synthetase from Escherichia coli: Functional Evidence for Cross-Dimer tRNA Binding during Aminoacylation","volume":"23","author":"Vincent","year":"1995","journal-title":"Nucl. Acids Res."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"8009","DOI":"10.1073\/pnas.0903229106","article-title":"An ABC Transport System That Maintains Lipid Asymmetry in the Gram-Negative Outer Membrane","volume":"106","author":"Malinverni","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"E1565","DOI":"10.1073\/pnas.1601375113","article-title":"Disruption of Lipid Homeostasis in the Gram-Negative Cell Envelope Activates a Novel Cell Death Pathway","volume":"113","author":"Sutterlin","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1616","DOI":"10.1038\/s41564-017-0046-x","article-title":"Structural Basis for Maintenance of Bacterial Outer Membrane Lipid Asymmetry","volume":"2","author":"Kaptan","year":"2017","journal-title":"Nat. Microbiol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1007\/s00253-021-11708-x","article-title":"Resistance Response to Arenicin Derivatives in Escherichia coli","volume":"106","author":"Wang","year":"2022","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1007\/s12275-024-00137-w","article-title":"Structural Insights into the Lipopolysaccharide Transport (Lpt) System as a Novel Antibiotic Target","volume":"62","author":"Yoon","year":"2024","journal-title":"J. Microbiol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"5363","DOI":"10.1073\/pnas.0912872107","article-title":"Characterization of the Two-Protein Complex in Escherichia coli Responsible for Lipopolysaccharide Assembly at the Outer Membrane","volume":"107","author":"Chng","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"eaau2634","DOI":"10.1126\/sciadv.aau2634","article-title":"Thanatin Targets the Intermembrane Protein Complex Required for Lipopolysaccharide Transport in Escherichia coli","volume":"4","author":"Vetterli","year":"2018","journal-title":"Sci. Adv."},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"Panteleev, P.V., Safronova, V.N., Kruglikov, R.N., Bolosov, I.A., and Ovchinnikova, T.V. (2023). Genomic Insights into Bacterial Resistance to Proline-Rich Antimicrobial Peptide Bac7. Membranes, 13.","DOI":"10.3390\/membranes13040438"},{"key":"ref_26","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 \u03b2-Hairpin Antimicrobial Peptide Capitellacin from the Marine Polychaeta Capitella teleta. Mar. Drugs, 20.","DOI":"10.3390\/md20030167"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1007\/978-1-0716-0954-5_17","article-title":"Microscale Thermophoresis (MST) to Detect the Interaction Between Purified Protein and Small Molecule","volume":"Volume 2213","author":"Hicks","year":"2021","journal-title":"Plant Chemical Genomics"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"042001","DOI":"10.1088\/2050-6120\/ac82a6","article-title":"Microscale Thermophoresis as a Powerful Growing Analytical Technique for the Investigation of Biomolecular Interaction and the Determination of Binding Parameters","volume":"10","author":"Khan","year":"2022","journal-title":"Methods Appl. Fluoresc."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1130","DOI":"10.3390\/ph6091130","article-title":"What Goes around Comes Around\u2014A Comparative Study of the Influence of Chemical Modifications on the Antimicrobial Properties of Small Cyclic Peptides","volume":"6","author":"Scheinpflug","year":"2013","journal-title":"Pharmaceuticals"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"6327","DOI":"10.1038\/s41598-018-24154-z","article-title":"Fluorophore Labeling of a Cell-Penetrating Peptide Significantly Alters the Mode and Degree of Biomembrane Interaction","volume":"8","author":"Hedegaard","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"e00511\u201319","DOI":"10.1128\/AAC.00511-19","article-title":"Mutations in pmrB Confer Cross-Resistance between the LptD Inhibitor POL7080 and Colistin in Pseudomonas aeruginosa","volume":"63","author":"Romano","year":"2019","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1021\/la504407v","article-title":"Effect of Divalent Cation Removal on the Structure of Gram-Negative Bacterial Outer Membrane Models","volume":"31","author":"Clifton","year":"2015","journal-title":"Langmuir"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1898","DOI":"10.1021\/jm900999h","article-title":"Structure\u2212Activity Relationships of Polymyxin Antibiotics","volume":"53","author":"Velkov","year":"2010","journal-title":"J. Med. Chem."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1568","DOI":"10.1128\/AAC.46.5.1568-1570.2002","article-title":"Lack of Interaction of Fluoroquinolones with Lipopolysaccharides","volume":"46","author":"Lindner","year":"2002","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"17795","DOI":"10.1038\/s41598-017-18102-6","article-title":"Structure and Interactions of A Host Defense Antimicrobial Peptide Thanatin in Lipopolysaccharide Micelles Reveal Mechanism of Bacterial Cell Agglutination","volume":"7","author":"Sinha","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"1625","DOI":"10.1038\/s41467-022-29234-3","article-title":"A Synthetic Lipopeptide Targeting Top-Priority Multidrug-Resistant Gram-Negative Pathogens","volume":"13","author":"Roberts","year":"2022","journal-title":"Nat. Commun."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"a025247","DOI":"10.1101\/cshperspect.a025247","article-title":"\u03b2-Lactams and \u03b2-Lactamase Inhibitors: An Overview","volume":"6","author":"Bush","year":"2016","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"a027029","DOI":"10.1101\/cshperspect.a027029","article-title":"Aminoglycosides: An Overview","volume":"6","author":"Krause","year":"2016","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"368","DOI":"10.1016\/j.bpj.2017.10.046","article-title":"Melittin-Induced Permeabilization, Re-Sealing, and Re-Permeabilization of E. coli Membranes","volume":"114","author":"Yang","year":"2018","journal-title":"Biophys. J."},{"key":"ref_40","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_41","doi-asserted-by":"crossref","unstructured":"Yasir, M., Dutta, D., and Willcox, M.D.P. (2019). Mode of Action of the Antimicrobial Peptide Mel4 Is Independent of Staphylococcus aureus Cell Membrane Permeability. PLoS ONE, 14.","DOI":"10.1101\/603712"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"e01056\u201316","DOI":"10.1128\/AAC.01056-16","article-title":"Combined Systems Approaches Reveal a Multistage Mode of Action of a Marine Antimicrobial Peptide against Pathogenic Escherichia coli and Its Protective Effect against Bacterial Peritonitis and Endotoxemia","volume":"61","author":"Wang","year":"2017","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"8925","DOI":"10.1038\/s41467-024-53309-y","article-title":"Rumicidins Are a Family of Mammalian Host-Defense Peptides Plugging the 70S Ribosome Exit Tunnel","volume":"15","author":"Panteleev","year":"2024","journal-title":"Nat. Commun."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1385\/1-59259-809-9:353","article-title":"Automated NMR Structure Calculation with CYANA","volume":"Volume 278","year":"2004","journal-title":"Protein NMR Techniques"}],"container-title":["Marine Drugs"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1660-3397\/24\/5\/154\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,5,15]],"date-time":"2026-05-15T04:13:57Z","timestamp":1778818437000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1660-3397\/24\/5\/154"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,4,27]]},"references-count":44,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2026,5]]}},"alternative-id":["md24050154"],"URL":"https:\/\/doi.org\/10.3390\/md24050154","relation":{},"ISSN":["1660-3397"],"issn-type":[{"value":"1660-3397","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,4,27]]}}}