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Opioid Receptor Ligands Derived from Food Proteins

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During the last two decades a variety of food protein fragments has been demonstrated to elicit biological effects in various in vitro or in vivo test systems. A considerable part of these bioactive peptides are opioid receptor ligands , which may be regarded as exogenous supplements to the endogenous opioidergic systems of the human organism. Most of these foodderived opioid receptor ligands are fragments of the milk proteins alpha-, beta- or kappa-casein, alpha-lactalbumin, beta-lactoglobulin or lactotransferrin; however, also wheat gluten, rice albumin, bovine serum albumin or hemoglobin, i.e. possible constituents of meat, and even a protein from spinach could be demonstrated to contain fragments behaving like opioid receptor ligands. Practically all of these compounds display opioid agonist activity; only very few of them behave like opioid antagonists. Bioactive food protein derivatives have been termed “ food hormones”, which implies that these compounds display their bioactivities when released from food constituents, i.e. from their precursor molecules due to the action of gastrointestinal enzymes. The critical point in case of food protein-derived opioid receptor ligands is that only a minority of their bioactive effects demonstrated as yet has been observed upon oral or intragastric administration of these peptides or their precursor proteins and that most of these studies have been performed in animals. Thus, in terms of “evidence-based dietary supplementation” more studies are needed to prove effects of food protein-derived opioid receptor ligands or their precursors after oral administration in humans and, moreover, to prove a benefit for the consumer's organism.





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Keywords: beta-casomorphins; bioactive substances; functional food; gluten exorphins; hemorphins; opioid peptides; opioid receptor ligands; opioids

Document Type: Review Article

Publication date: June 1, 2003

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