Opioid peptides encrypted in intact milk protein sequences

Br J Nutr. 2000 Nov;84 Suppl 1:S27-31. doi: 10.1017/s000711450000221x.

Abstract

Opioid agonistic and antagonistic peptides which are inactive within the sequence of the precursor milk proteins can be released and thus activated by enzymatic proteolysis, for example during gastrointestinal digestion or during food processing. Activated opioid peptides are potential modulators of various regulatory processes in the body. Opioid peptides can interact with subepithelial opioid receptors or specific luminal binding sites in the intestinal tract. Furthermore, they may be absorbed and then reach endogenous opioid receptors.

Publication types

  • Review

MeSH terms

  • Animal Nutritional Physiological Phenomena
  • Animals
  • Biological Products / therapeutic use
  • Caseins / metabolism
  • Endorphins / genetics
  • Endorphins / metabolism
  • Humans
  • Intestinal Absorption
  • Mammals
  • Milk Proteins / chemistry*
  • Opioid Peptides / chemistry*
  • Opioid Peptides / physiology
  • Peptide Hydrolases / metabolism
  • Recombinant Proteins / administration & dosage

Substances

  • Biological Products
  • Caseins
  • Endorphins
  • Milk Proteins
  • Opioid Peptides
  • Recombinant Proteins
  • beta-casomorphins
  • Peptide Hydrolases