On the structural stability of a small bioactive peptide of potential use in biotechnology

J Biomol Struct Dyn. 1999 Apr;16(5):1053-9. doi: 10.1080/07391102.1999.10508314.

Abstract

A tridecapeptide with the sequence CCEICCNPACFGC has been synthesized to reproduce the active moiety of a heat stable enterotoxin from Vibrio cholerae. The proton NMR analysis indicates, for the active synthetic fragment, a rigid secondary structure stabilised by three disulfide bridges. Such a rigid peptide, suitably detoxified and activated, could be a good candidate to be used as a carrier for linear bioactive peptides or other functional groups.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biotechnology / methods*
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Peptides / chemistry*
  • Protein Conformation
  • Protein Structure, Secondary*

Substances

  • Peptides