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Antimicrobial Peptides: Amphibian Host Defense Peptides

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62690094%3A18470%2F19%3A50016123" target="_blank" >RIV/62690094:18470/19:50016123 - isvavai.cz</a>

  • Alternative codes found

    RIV/60076658:12110/19:43897803 RIV/00179906:_____/19:10403235

  • Result on the web

    <a href="https://www.ingentaconnect.com/content/ben/cmc/2019/00000026/00000032/art00004;jsessionid=25nq1j1k6ii4n.x-ic-live-01" target="_blank" >https://www.ingentaconnect.com/content/ben/cmc/2019/00000026/00000032/art00004;jsessionid=25nq1j1k6ii4n.x-ic-live-01</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.2174/0929867325666180713125314" target="_blank" >10.2174/0929867325666180713125314</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Antimicrobial Peptides: Amphibian Host Defense Peptides

  • Original language description

    Antimicrobial 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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    30104 - Pharmacology and pharmacy

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2019

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Current medicinal chemistry

  • ISSN

    0929-8673

  • e-ISSN

  • Volume of the periodical

    26

  • Issue of the periodical within the volume

    32

  • Country of publishing house

    AE - UNITED ARAB EMIRATES

  • Number of pages

    23

  • Pages from-to

    5924-5946

  • UT code for WoS article

    000497819700003

  • EID of the result in the Scopus database

    2-s2.0-85075676552