Chemical Synthesis and Biological Activity of the Gelatinase Biosynthesis-Activating Pheromone of Enterococcus Faecalis and Its Analogs

Biosci Biotechnol Biochem. 2001 Oct;65(10):2322-5. doi: 10.1271/bbb.65.2322.

Abstract

An 11-residue peptide lactone, termed the gelatinase biosynthesis-activating pheromone (GBAP), triggers the production of the pathogenicity-related extracellular proteases, gelatinase and serine protease, in Enterococcus faecalis. In this study, we synthesized GBAP and its analogs and examined their gelatinase biosynthesis-inducing activity. This study on the structure-activity relationship shows that a lactone ring was indispensable for the activity.

MeSH terms

  • Amino Acid Sequence
  • Enterococcus faecalis / metabolism*
  • Lactones / chemical synthesis*
  • Lactones / pharmacology*
  • Peptides, Cyclic / chemical synthesis*
  • Peptides, Cyclic / pharmacology*
  • Pheromones / chemical synthesis*
  • Pheromones / pharmacology*
  • Structure-Activity Relationship

Substances

  • Lactones
  • Peptides, Cyclic
  • Pheromones
  • gelatinase biosynthesis-activating pheromone