Tethering antimicrobial peptides: current status and potential challenges

Biotechnol Adv. 2011 Jan-Feb;29(1):67-74. doi: 10.1016/j.biotechadv.2010.08.012. Epub 2010 Sep 9.

Abstract

Antimicrobial peptides (AMPs) are next generation antibiotics which will make excellent coating agents for a myriad of devices because they are far less susceptible to the development of pathogen resistance compared to conventional antibiotics, exhibit rapid and broad-spectrum killing profiles, and are effective at low concentrations. These advantages, however, are compromised upon AMP tethering to solid supports. The effects of peptide-tethering strategies in governing AMP orientation, surface density, flexibility, and activity are reviewed. Understanding AMP structure-function relationship in the tethered conformation will enable rational improvements of immobilisation parameters. Foreseeable challenges in the development of AMP-coated devices such as microbial accumulation on implant surface and the lack of direct biomolecular structure and orientation data of peptides on surfaces are also discussed, and solutions to address these roadblocks are also proposed.

Publication types

  • Review

MeSH terms

  • Antimicrobial Cationic Peptides / chemistry
  • Antimicrobial Cationic Peptides / pharmacology*
  • Coated Materials, Biocompatible / pharmacology*
  • Humans
  • Immobilized Proteins / pharmacology*
  • Prostheses and Implants / microbiology

Substances

  • Antimicrobial Cationic Peptides
  • Coated Materials, Biocompatible
  • Immobilized Proteins