Stability against enzymatic hydrolysis of endomorphin-1 analogues containing beta-proline

Org Biomol Chem. 2003 May 7;1(9):1498-502. doi: 10.1039/b301507f.

Abstract

The enantiomer of endomorphin-1 (Tyr-Pro-Trp-PheNH2) and the analogues containing (S)- or (R)-beta-proline have been synthesized, and their affinities towards mu-opioid receptors have been measured. As expected, the incubations of the different peptides with some commercially available enzymes showed that the presence of D-residues gave strong resistance towards digestion. The presence of beta-proline alone is sufficient to confer good resistance against the hydrolysis of the biologically strategic Pro-Trp bond.

Publication types

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

MeSH terms

  • Animals
  • CD13 Antigens / metabolism
  • Carboxypeptidases / metabolism
  • Chymotrypsin / metabolism
  • Hydrolysis
  • Oligopeptides / chemical synthesis
  • Oligopeptides / chemistry*
  • Oligopeptides / metabolism*
  • Proline / chemistry*
  • Rats
  • Receptors, Opioid, mu / agonists
  • Stereoisomerism
  • Tryptophan / chemistry

Substances

  • Oligopeptides
  • Receptors, Opioid, mu
  • endomorphin 1
  • Tryptophan
  • Proline
  • Carboxypeptidases
  • CD13 Antigens
  • Chymotrypsin