Peptides Selected Using Phage Library Variants, Effectively Inhibit Trypanosoma cruzi Infection

Bull Exp Biol Med. 2017 Jul;163(3):361-364. doi: 10.1007/s10517-017-3804-0. Epub 2017 Jul 25.

Abstract

Four peptide sequences characterized by high content of hydrophobic, charged, and polar amino acids were obtained from 23 clones of M13 phage. Peptides P2 and P4 exhibited highest binding affinity for immobilized trypomastigotes. The inhibitory effects of peptides seemed to be due to blockade of certain epitopes on T. cruzi surface proteins responsible for interactions with the respective receptors of host cells.

Keywords: Trypanosoma cruzi; anti-infectious activity; peptides.

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Biotinylation
  • HeLa Cells
  • Humans
  • Life Cycle Stages / drug effects*
  • Life Cycle Stages / physiology
  • Oligopeptides / metabolism
  • Oligopeptides / pharmacology*
  • Peptide Library*
  • Protein Binding
  • Trypanocidal Agents / metabolism
  • Trypanocidal Agents / pharmacology*
  • Trypanosoma cruzi / drug effects*
  • Trypanosoma cruzi / growth & development
  • Trypanosoma cruzi / metabolism

Substances

  • Oligopeptides
  • Peptide Library
  • Trypanocidal Agents