Tryptophan- and arginine-rich antimicrobial peptides: Anti-infectives with great potential.

Suzana K Straus
Author Information
  1. Suzana K Straus: Department of Chemistry, University of British Columbia, 2036 Main Mall, Vancouver, BC V6T 1Z1, Canada. Electronic address: sstraus@chem.ubc.ca.

Abstract

With the increasing prevalence of multidrug resistant (MDR) bacteria, there is a need to design synthetic antimicrobial peptides (AMPs) that are effective and selective for bacteria, i.e. non-toxic to mammalian cells. One design strategy, namely the use of tryptophan- and arginine-rich AMPs, is rooted in the study of natural AMPs that are composed mainly of these amino acids, such as lactoferricin, tritrpticin, and puroindoline. A number of important studies on these AMPs by the Vogel group are reviewed here. More recent work on W-/R-rich peptides is also presented. The examples show that these peptides represent anti-infectives with great potential.

Keywords

MeSH Term

Animals
Tryptophan
Arginine
Antimicrobial Peptides
Anti-Infective Agents
Peptides
Mammals

Chemicals

Tryptophan
Arginine
Antimicrobial Peptides
Anti-Infective Agents
Peptides

Word Cloud

Created with Highcharts 10.0.0peptidesAMPsdesignbacteriaantimicrobialarginine-richgreatpotentialincreasingprevalencemultidrugresistantMDRneedsyntheticeffectiveselectiveienon-toxicmammaliancellsOnestrategynamelyusetryptophan-rootedstudynaturalcomposedmainlyaminoacidslactoferricintritrpticinpuroindolinenumberimportantstudiesVogelgroupreviewedrecentworkW-/R-richalsopresentedexamplesshowrepresentanti-infectivesTryptophan-peptides:Anti-infectivesAntimicrobialArg/Trp-richCation-��interactionHostdefensePeptidesequence

Similar Articles

Cited By