{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,9]],"date-time":"2026-10-09T20:01:14Z","timestamp":1791576074144,"version":"4.3.4"},"reference-count":226,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2023,2,19]],"date-time":"2023-02-19T00:00:00Z","timestamp":1676764800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"S\u00e3o Paulo Research Foundation\u2014FAPESP","award":["2015\/00003-5 (NO)"],"award-info":[{"award-number":["2015\/00003-5 (NO)"]}]},{"name":"S\u00e3o Paulo Research Foundation\u2014FAPESP","award":["2022\/01825-2 (MTM)"],"award-info":[{"award-number":["2022\/01825-2 (MTM)"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Animals"],"abstract":"<jats:p>This review focuses on proteins and peptides with antimicrobial activity because these biopolymers can be useful in the fight against infectious diseases and to overcome the critical problem of microbial resistance to antibiotics. In fact, snakes show the highest diversification among reptiles, surviving in various environments; their innate immunity is similar to mammals and the response of their plasma to bacteria and fungi has been explored mainly in ecological studies. Snake venoms are a rich source of components that have a variety of biological functions. Among them are proteins like lectins, metalloproteinases, serine proteinases, L-amino acid oxidases, phospholipases type A2, cysteine-rich secretory proteins, as well as many oligopeptides, such as waprins, cardiotoxins, cathelicidins, and \u03b2-defensins. In vitro, these biomolecules were shown to be active against bacteria, fungi, parasites, and viruses that are pathogenic to humans. Not only cathelicidins, but all other proteins and oligopeptides from snake venom have been proteolyzed to provide short antimicrobial peptides, or for use as templates for developing a variety of short unnatural sequences based on their structures. In addition to organizing and discussing an expressive amount of information, this review also describes new \u03b2-defensin sequences of Sistrurus miliarius that can lead to novel peptide-based antimicrobial agents, using a multidisciplinary approach that includes sequence phylogeny.<\/jats:p>","DOI":"10.3390\/ani13040744","type":"journal-article","created":{"date-parts":[[2023,2,20]],"date-time":"2023-02-20T05:57:52Z","timestamp":1676872672000},"page":"744","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":18,"title":["Past, Present, and Future of Naturally Occurring Antimicrobials Related to Snake Venoms"],"prefix":"10.3390","volume":"13","author":[{"given":"Nancy","family":"Oguiura","sequence":"first","affiliation":[{"name":"Laboratory of Ecology and Evolution, Instituto Butantan, Av. Dr. Vital Brasil 1500, S\u00e3o Paulo 05503-900, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Leonardo","family":"Sanches","sequence":"additional","affiliation":[{"name":"Laboratory of Ecology and Evolution, Instituto Butantan, Av. Dr. Vital Brasil 1500, S\u00e3o Paulo 05503-900, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Priscila V.","family":"Duarte","sequence":"additional","affiliation":[{"name":"Laboratory of Ecology and Evolution, Instituto Butantan, Av. Dr. Vital Brasil 1500, S\u00e3o Paulo 05503-900, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9056-0068","authenticated-orcid":false,"given":"Marcos A.","family":"Sulca-L\u00f3pez","sequence":"additional","affiliation":[{"name":"Aquatic Microbiology and Technological Applications, Department of Microbiology and Parasitology, Faculty of Biological Sciences, Universidad Nacional Mayor de San Marcos, Av. Venezuela Cdra. 34 s\/n, Ciudad Universitaria, Lima 15081, Peru"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5772-004X","authenticated-orcid":false,"given":"Maria Ter\u00easa","family":"Machini","sequence":"additional","affiliation":[{"name":"Laboratory of Peptide Chemistry, Department of Biochemistry, Institute of Chemistry, University of S\u00e3o Paulo, Av. Prof. Lineu Prestes, 748, S\u00e3o Paulo 05508-000, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,2,19]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1038\/415389a","article-title":"Antimicrobial peptides of multicellular organisms","volume":"415","author":"Zasloff","year":"2002","journal-title":"Nature"},{"key":"ref_2","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. 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