An Atlas of Anionic Antimicrobial Peptides from Amphibians

Curr Protein Pept Sci. 2018;19(8):823-838. doi: 10.2174/1389203719666180226155035.

Abstract

Anionic antimicrobial peptides (AAMPs) with net charges ranging from -1 to -8 have been identified in frogs, toads, newts and salamanders across Africa, South America and China. Most of these peptides show antibacterial activity and a number of them are multifunctional, variously showing antifungal activity, anticancer action, neuropeptide function and the ability to potentiate conventional antibiotics. Antimicrobial mechanisms proposed for these AAMPs, include toroidal pore formation and the Shai-Huang-Matsazuki model of membrane interaction along with pH dependent amyloidogenesis and membranolysis via tilted peptide formation. The potential for therapeutic and biotechnical application of these AAMPs has been demonstrated, including the development of amyloid-based nanomaterials and antiviral agents. It is concluded that amphibian AAMPs represent an untapped potential source of biologically active agents and merit far greater research interest.

Keywords: Anionic antimicrobial peptides; amphibian; amyloid; amyloidogenesis; anticancer; membranolysis..

Publication types

  • Review

MeSH terms

  • Africa
  • Amphibian Proteins / chemistry*
  • Amphibian Proteins / pharmacology*
  • Amphibian Proteins / therapeutic use
  • Amphibians / metabolism*
  • Amyloid / metabolism
  • Animals
  • Anions / chemistry
  • Anti-Bacterial Agents / chemistry
  • Anti-Bacterial Agents / pharmacology
  • Anti-Bacterial Agents / therapeutic use
  • Antineoplastic Agents / chemistry
  • Antineoplastic Agents / pharmacology
  • Antineoplastic Agents / therapeutic use
  • Antiviral Agents / chemistry
  • Antiviral Agents / pharmacology
  • China
  • Humans
  • Peptides / chemistry*
  • Peptides / pharmacology*
  • Peptides / therapeutic use
  • Protein Binding
  • Signal Transduction
  • South America

Substances

  • Amphibian Proteins
  • Amyloid
  • Anions
  • Anti-Bacterial Agents
  • Antineoplastic Agents
  • Antiviral Agents
  • Peptides