Synthesis and biological properties of carba-analogs of heat-stable enterotoxin (ST) produced by enterotoxigenic Escherichia coli

Biochem Biophys Res Commun. 1991 May 15;176(3):958-65. doi: 10.1016/0006-291x(91)90375-h.

Abstract

Analogs of a heat-stable enterotoxin (ST) that have a CH2-S linkage instead of an S-S linkage in the molecule were synthesized by conventional methods. The synthetic peptides showed toxicity, assayed as induction of fluid secretion in suckling mice, although their toxicities were hundredth that of native ST. This finding implies that ST is not recognized by its receptor protein through an exchange reaction between its disulfide linkages and thiol-groups of its receptor protein(s), but through hydrophobic or electrostatic interactions.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bacterial Toxins / chemical synthesis*
  • Bacterial Toxins / metabolism
  • Bacterial Toxins / toxicity
  • Chromatography, High Pressure Liquid
  • Electrophoresis, Polyacrylamide Gel
  • Enterotoxins / chemical synthesis*
  • Enterotoxins / metabolism
  • Enterotoxins / toxicity
  • Escherichia coli
  • Escherichia coli Proteins
  • Guanylate Cyclase*
  • Indicators and Reagents
  • Mice
  • Microvilli / metabolism
  • Molecular Sequence Data
  • Peptides / chemical synthesis
  • Peptides / metabolism
  • Peptides / toxicity
  • Rats
  • Rats, Inbred Strains
  • Receptors, Cell Surface / metabolism
  • Receptors, Enterotoxin
  • Receptors, Guanylate Cyclase-Coupled
  • Receptors, Peptide*
  • Structure-Activity Relationship

Substances

  • Bacterial Toxins
  • Enterotoxins
  • Escherichia coli Proteins
  • Indicators and Reagents
  • Peptides
  • Receptors, Cell Surface
  • Receptors, Peptide
  • heat stable toxin (E coli)
  • Guanylate Cyclase
  • Receptors, Enterotoxin
  • Receptors, Guanylate Cyclase-Coupled