IMR Press / FBL / Volume 21 / Issue 7 / DOI: 10.2741/4461

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.


Antimicrobial peptides from frog skin: biodiversity and therapeutic promises

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1 Sorbonne Universites, UPMC Univ Paris 06, FR 3631, Institut de Biologie Paris Seine (IBPS), Biogenese des Signaux Peptidiques (BIOSIPE), F-75005, Paris, France UPMC, France
2 CNRS, FR 3631, IBPS, BIOSIPE, F-75005, Paris, France UPMC, France
3 Sorbonne Universites, UPMC Univ Paris 06, France
Front. Biosci. (Landmark Ed) 2016, 21(7), 1341–1371;
Published: 1 June 2016

More than a thousand antimicrobial peptides (AMPs) have been reported in the last decades arising from the skin secretion of amphibian species. Generally, each frog species can express its own repertoire of AMPs (typically, 10–20 peptides) with differing sequences, sizes, and spectrum of action, which implies very rapid divergence, even between closely related species. Frog skin AMPs are highly potent against antibiotic-resistant bacteria, protozoa, yeasts, and fungi by permeating and destroying their plasma membrane and/or inactivating intracellular targets. These peptides have attracted considerable interest as a therapeutic alternative to conventional anti-infective agents. However, efforts to obtain a new generation of drugs using these peptides are still challenging because of high associated R&D costs due to their large size (up to 46 residues) and cytotoxicity. This review deals with the biodiversity of frog skin AMPs and assesses the therapeutic possibilities of temporins, the shortest AMPs found in the frog skin, with 8-17 residues. Such short sequences are easily amenable to optimization of the structure and to solution-phase synthesis that offer reduced costs over solid-phase chemistry.

Frog Skin
Antimicrobial Peptides
Host Defense Peptides
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