Short Cationic Peptide Derived from Archaea with Dual Antibacterial Properties and Anti-Infective Potential

ACS Infect Dis. 2019 Jul 12;5(7):1081-1086. doi: 10.1021/acsinfecdis.9b00073. Epub 2019 May 1.

Abstract

Bacterial biofilms and associated infections represent one of the biggest challenges in the clinic, and as an alternative to counter bacterial infections, antimicrobial peptides have attracted great attention in the past decade. Here, ten short cationic antimicrobial peptides were generated through a sliding-window strategy on the basis of the 19-amino acid residue peptide, derived from a Pyrobaculum aerophilum ribosomal protein. PaDBS1R6F10 exhibited anti-infective potential as it decreased the bacterial burden in murine Pseudomonas aeruginosa cutaneous infections by more than 1000-fold. Adverse cytotoxic and hemolytic effects were not detected against mammalian cells. The peptide demonstrated structural plasticity in terms of its secondary structure in the different environments tested. PaDBS1R6F10 represents a promising antimicrobial agent against bacteria infections, without harming human cells.

Keywords: CD spectroscopy; antimicrobial peptide; biofilm; cutaneous infection.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antimicrobial Cationic Peptides / chemistry
  • Antimicrobial Cationic Peptides / pharmacology*
  • Archaeal Proteins / chemistry
  • Biofilms / drug effects
  • Biofilms / growth & development
  • Disease Models, Animal
  • Humans
  • Mice
  • Microbial Sensitivity Tests
  • Protein Structure, Secondary
  • Pseudomonas Infections / drug therapy*
  • Pseudomonas aeruginosa / drug effects*
  • Pseudomonas aeruginosa / physiology
  • Pyrobaculum / metabolism*
  • Ribosomal Proteins / chemistry*

Substances

  • Antimicrobial Cationic Peptides
  • Archaeal Proteins
  • Ribosomal Proteins