Fighting microbial infections: A lesson from amphibian skin-derived esculentin-1 peptides

Peptides. 2015 Sep:71:286-95. doi: 10.1016/j.peptides.2015.04.018. Epub 2015 May 8.

Abstract

Due to the growing emergence of resistance to commercially available antibiotics/antimycotics in virtually all clinical microbial pathogens, the discovery of alternative anti-infective agents, is greatly needed. Gene-encoded antimicrobial peptides (AMPs) hold promise as novel therapeutics. In particular, amphibian skin is one of the richest storehouses of AMPs, especially that of the genus Rana, with esculentins-1 being among the longest (46 amino acids) AMPs found in nature to date. Here, we report on the recently discovered in vitro and in vivo activities and mechanism of action of two derivatives of the N-terminal part of esculentin-1a and -1b peptides, primarily against two relevant opportunistic microorganisms causing a large number of life-threatening infections worldwide; i.e. the Gram-negative bacterium Pseudomonas aeruginosa and the yeast Candida albicans. Because of distinct advantages compared to several mammalian AMPs, the two selected frog skin AMP-derivatives represent attractive candidates for the development of new antimicrobial compounds with expanded properties, for both human and veterinary medicine.

Keywords: Antimicrobial peptide; Cystic fibrosis; Frog skin; Infectious diseases; Innate immunity; Keratitis.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amphibian Proteins / chemistry
  • Amphibian Proteins / pharmacology*
  • Animals
  • Anti-Infective Agents / chemistry
  • Anti-Infective Agents / pharmacology*
  • Antimicrobial Cationic Peptides / chemistry
  • Antimicrobial Cationic Peptides / pharmacology*
  • Candida / growth & development*
  • Candidiasis / drug therapy*
  • Humans
  • Pseudomonas Infections / drug therapy*
  • Pseudomonas aeruginosa / growth & development*
  • Ranidae
  • Skin / chemistry*

Substances

  • Amphibian Proteins
  • Anti-Infective Agents
  • Antimicrobial Cationic Peptides
  • esculentin protein, Rana esculenta