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Casomorphin is an opioid peptide (protein fragment) derived from the digestion of the milk protein casein. [1]
Digestive enzymes can break casein down into peptides that have some biological activity in cells and in laboratory animals though conclusive causal effects on humans have not been established. [1]
Some practitioners of alternative medicine claim that casomorphin may cause some of the symptoms of autism, and promote casein exclusion diets as a supposed cure, as of 2008 [update] there was a lack of evidence that these diets had any effect. [2]
If opioid peptides breach the intestinal barrier, typically linked to permeability and constrained biosynthesis of dipeptidyl peptidase-4 (DPP4), they can attach to opioid receptors. Elucidation requires a systemic framework that acknowledges that public-health effects of food-derived opioids are complex with varying genetic susceptibility and confounding factors, together with system-wide interactions and feedbacks. [3]
bBCM7 is produced in when digesting bovine A1 beta-casein outside of the body using pancreatic enzymes, and inside of some animal bodies. The A2 form, which follows Ile with a Pro instead of a His, is more resistant to the release of bBCM7, presumably because the proline residue blocks the action of a carboxyl peptidase. bBCM7 has significant opioid effects when injected (and in more recent research, orally fed) into animals, [3] but human studies supporting the use of "bBCM7-free" A2 milk is still lacking. [1]
Despite human beta-casein having a A2-like "P" after "I", human colostrum and early lactation-stage milk contains significant amounts of hBCM7. It is a much weaker opioid and the FVQ sequence renders it susceptible to further degradation. [3]
X is H (histidine) in A1 and P (proline) in A2.
X is H (histidine) in A1 and P (proline) in A2.
Produced from both A1 and A2. Opioid agonist, but apparently without the detrimental effect of bBCM7 in cell cultures and animal models, and in fact considered potentially beneficial. [3]