Show simple item record

dc.contributor.authorPatočka, Jiřícze
dc.contributor.authorNepovimová, E.cze
dc.contributor.authorKlímová, B.cze
dc.contributor.authorWu, Q.cze
dc.contributor.authorKuča, K.cze
dc.date.accessioned2021-03-04T17:30:24Z
dc.date.available2021-03-04T17:30:24Z
dc.date.issued2019eng
dc.identifier.issn0929-8673eng
dc.identifier.urihttps://dspace.jcu.cz/handle/20.500.14390/516
dc.description.abstractAntimicrobial peptides (AMPs) are one of the most common components of the innate immune system that protect multicellular organisms against microbial invasion. The vast majority of AMPs are isolated from the frog skin. Anuran (frogs and toads) skin contains abundant AMPs that can be developed therapeutically. Such peptides are a unique but diverse group of molecules. In general, more than 50% of the amino acid residues form the hydrophobic part of the molecule. Normally, there are no conserved structural motifs responsible for activity, although the vast majority of the AMPs are cationic due to the presence of multiple lysine residues; this cationicity has a close relationship with antibacterial activity. Notably, recent evidence suggests that synthesis of AMPs in frog skin may confer an advantage on a particular species, although they are not essential for survival. Frog skin AMPs exert potent activity against antibiotic-resistant bacteria, protozoa, yeasts, and fungi by permeating and destroying the plasma membrane and inactivating intracellular targets. Importantly, since they do not bind to a specific receptor, AMPs are less likely to induce resistance mechanisms. Currently, the best known amphibian AMPs are esculentins, brevinins, ranacyclins, ranatuerins, nigrocin-2, magainins, dermaseptins, bombinins, temporins, and japonicins-1 and -2, and palustrin-2. This review focuses on these frog skin AMPs and the mechanisms underlying their antimicrobial activity. We hope that this review will provide further information that will facilitate further study of AMPs and cast new light on novel and safer microbicides.eng
dc.formatp. 5924-5946eng
dc.language.isoengeng
dc.publisherBentham Science Publishers Ltd.eng
dc.relation.ispartofCurrent Medicinal Chemistry, volume 26, issue: 32eng
dc.subjectAntimicrobial peptideeng
dc.subjectAMPseng
dc.subjectantibacterialeng
dc.subjectamphibian defense peptideseng
dc.subjectesculentinseng
dc.subjectbrevininseng
dc.subjectranacyclinseng
dc.subjectranatuerins.eng
dc.titleAntimicrobial Peptides: Amphibian Host Defense Peptideseng
dc.typearticleeng
dc.identifier.obd43883327eng
dc.peerreviewedyeseng
dc.publicationstatuspostprinteng
dc.identifier.doi10.2174/0929867325666180713125314eng
dc.relation.publisherversionhttps://www.ingentaconnect.com/content/ben/cmc/2019/00000026/00000032/art00004;jsessionid=20ruusm4o8m4w.x-ic-live-02?crawler=true&mimetype=application/pdfeng


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record