Abstract
Peptides with opioid activity have been described in partial enzymatic digests of proteins derived from foodstuffs and isolated from pepsin hydrolysates of wheat gluten, α- and β-casein [1]. Their appear quite resistant to the action of gastrointestinal enzymes. Therefore, once formed in the stomach, they could resist further degradation and elicit a physiological effect. The β-casomorphin sequence seems, to be of general occurrence in all the β-caseins so far investigated, although the structure of human β-casein slightly differs from that of its bovine counterpart. The differences occur within the β-casomorphin sequence for opiod activity. Thus, although the N-terminal tripeptide structure essential for opiod activity is conserved, human β-caseins are less potent than bovine β-casomorphins in the GPI assay [2]. βCasomorphins show specific binding to μ-receptors probably due to their sequence Tyr-Pro-Phe. Apart from their possible role as neuro-transmitters and neuromodulators, β-casomorphins may also influence neutral maturation, since pre-natal and post-natal administration of opiate receptor agonists can alter the development of various neutral pathways [3].
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© 1998 Springer Science+Business Media Dordrecht
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Chruscinska, E., Micera, G., Sanna, D., Ambroziak, W. (1998). Specific Interaction of β-Casomorphin (Human) with Cu(II) Ion. In: Coleman, A.W. (eds) Molecular Recognition and Inclusion. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-5288-4_41
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DOI: https://doi.org/10.1007/978-94-011-5288-4_41
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