A novel antimicrobial peptide from Bufo bufo gargarizans

Biochem Biophys Res Commun. 1996 Jan 5;218(1):408-13. doi: 10.1006/bbrc.1996.0071.

Abstract

A potent and structurally novel antimicrobial peptide was isolated and characterized from the stomach tissue of Bufo bufo gargarizans, an Asian toad. The 39-amino acid peptide, named buforin I, was purified to homogeneity by heparin-affinity column and reverse-phase HPLC. The amino acid sequence of buforin I was identical in 37 of 39 amino-terminal residues of Xenopus histone H2A. The buforin I showed strong antimicrobial activities in vitro against a broad-spectrum of microorganisms and was found to be more potent than magainin 2. In addition, a 21-amino acid peptide, named buforin II, which was derived from buforin I, showed more potent antimicrobial activities than buforin I.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Anti-Bacterial Agents
  • Anti-Infective Agents / chemistry
  • Anti-Infective Agents / isolation & purification*
  • Anti-Infective Agents / pharmacology
  • Bufo bufo*
  • Chromatography, Affinity
  • Chromatography, High Pressure Liquid
  • Fungi / drug effects
  • Gram-Negative Bacteria / drug effects
  • Gram-Positive Bacteria / drug effects
  • Histones / chemistry
  • Microbial Sensitivity Tests
  • Molecular Sequence Data
  • Molecular Weight
  • Proteins / chemistry
  • Proteins / isolation & purification*
  • Proteins / pharmacology
  • Sequence Homology, Amino Acid
  • Stomach / chemistry*
  • Xenopus

Substances

  • Anti-Bacterial Agents
  • Anti-Infective Agents
  • Histones
  • Proteins
  • buforin I
  • buforin II