Structure-function relationships in bombinins H, antimicrobial peptides from Bombina skin secretions

Peptides. 2000 Nov;21(11):1673-9. doi: 10.1016/s0196-9781(00)00316-8.

Abstract

Skin secretions of amphibia of the Bombina genus contain two families of antimicrobial peptides, the bombinins (bombinin-like peptides) and the bombinins H (H for hydrophobic and hemolytic). The latter family includes a number of peptides containing a D-amino acid in the second position, in addition to their corresponding all L-isomers. The antimicrobial activity of three pairs of bombinin H isomers, H2/H4, H6/H7 and GH-1D/GH-1L, has been investigated. The first two pairs of peptides were actually isolated from the secretion, whereas the third was synthesized according to the sequence deduced from a gene coding for a bombinin-like peptide in Bombina orientalis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / chemistry
  • Animals
  • Anti-Bacterial Agents / pharmacology
  • Antimicrobial Cationic Peptides
  • Anura
  • Cell Membrane / drug effects
  • Cytoplasm / metabolism
  • Dose-Response Relationship, Drug
  • Erythrocytes / drug effects
  • Escherichia coli / drug effects
  • Humans
  • Peptides / chemistry*
  • Peptides / metabolism
  • Peptides / physiology
  • Potassium / metabolism
  • Skin / metabolism*
  • Stereoisomerism
  • Structure-Activity Relationship
  • Time Factors
  • Yersinia pseudotuberculosis / drug effects

Substances

  • Amino Acids
  • Anti-Bacterial Agents
  • Antimicrobial Cationic Peptides
  • Peptides
  • gene-drived bombinin H-like peptide
  • Potassium