Substrate specificity and screening of the integral membrane protease Pla

Bioorg Med Chem Lett. 2008 Jan 1;18(1):427-31. doi: 10.1016/j.bmcl.2007.09.104. Epub 2007 Oct 12.

Abstract

This paper reports a study to find small peptide substrates for the important virulence factor of Yersinia pestis, plasminogen activator, Pla. The method used to find small substrates for this protease is reported along with studies examining the ability of these peptides to inhibit activity of the enzyme. Through the use of parallel synthesis and positional scanning, small tripeptides were identified that are viable substrates for the protease.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / antagonists & inhibitors*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Fluorometry
  • Kinetics
  • Molecular Sequence Data
  • Oligopeptides / chemical synthesis
  • Oligopeptides / chemistry
  • Oligopeptides / pharmacology
  • Peptides / chemical synthesis*
  • Peptides / chemistry
  • Peptides / pharmacology*
  • Plasminogen Activators / antagonists & inhibitors*
  • Plasminogen Activators / chemistry
  • Plasminogen Activators / metabolism
  • Protease Inhibitors / chemical synthesis*
  • Protease Inhibitors / chemistry
  • Protease Inhibitors / pharmacology*
  • Protein Conformation
  • Structure-Activity Relationship
  • Substrate Specificity
  • Yersinia pestis / enzymology

Substances

  • Bacterial Proteins
  • Oligopeptides
  • Peptides
  • Protease Inhibitors
  • Pla protease, Yersinia pestis
  • Plasminogen Activators