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Opioide peptider fra matproteiner

Oversikt over peptider, struktur og kilde:

URL: Kjente opioide peptider fra matproteiner - kilde, struktur og kjemisk formel

 Biosci Biotechnol Biochem. 2007 Oct 7; [Epub ahead of print]Links
Soymorphins, Novel mu Opioid Peptides Derived from Soy beta-Conglycinin beta-Subunit, Have Anxiolytic Activities.
Ohinata K, Agui S, Yoshikawa M.
Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University.

Based on the amino acid sequence YPFV found in the soy beta-conglycinin beta-subunit, which is common to an opioid peptide human beta-casomorphin-4, peptides YPFVV, YPFVVN, and YPFVVNA were synthesized according to their primary structure. On guinea pig ileum (GPI) assay, they showed opioid activity (IC(50) = 6.0, 9.2 and 13 muM respectively) more potent than human beta-casomorphins, and were named soymorphins-5, -6, and -7, respectively. Their opioid activities on mouse vas deferens (MVD) assay were less potent than on GPI assay, suggesting that they are selective for the mu opioid receptor. Human beta-casomorphin-4 and soymorphin-5 were released from the soy 7S fraction (beta-conglycinin) by the action of gastrointestinal proteases. Soymorphins-5, -6, and -7 had anxiolytic activities after oral administration at doses of 10-30 mg/kg in the elevated plus-maze test in mice.

PMID: 17928679 [PubMed - as supplied by publisher]

Stanis³aw Kamiñski (1), Anna Cieoeliñska1, Elzbieta Kostyra (2)
1 Department of Animal Genetics, University of Warmia and Mazury, Olsztyn, Poland
2 Department of Biochemistry, University of Warmia and Mazury, Olsztyn, Poland
Polymorphism of bovine beta-casein and its potential effect on human health

Proteins in bovine milk are a common source of bioactive peptides. The peptides are released by the digestion of caseins and whey proteins. In vitro the bioactive peptide beta-casomorphin 7 (BCM-7) is yielded by the successive gastrointestinal proteolytic digestion of bovine beta-casein variants A1 and B, but this was not seen in variant A2. In hydrolysed milk with variant A1 of beta-casein, BCM-7 level is 4-fold higher than in A2 milk.

Variants A1 and A2 of beta-casein are common among many dairy cattle breeds. A1 is the most frequent in Holstein-Friesian (0.310–0.660), Ayrshire (0.432–0.720) and Red (0.710) cattle. In contrast, a high frequency of A2 is observed in Guernsey (0.880–0.970) and Jersey (0.490–0.721) cattle. BCM-7 may play a role in the aetiology of human diseases. Epidemiological evidence from New Zealand claims that consumption of beta-casein A1 is associated with higher national mortality rates from ischaemic heart disease. It seems that the populations that consume milk containing high levels of beta-casein A2 have a lower incidence of cardiovascular disease and type 1 diabetes. BCM-7 has also been suggested as a possible cause of sudden infant death syndrome. In addition, neurological disorders, such as autism and schizophrenia, seem to be associated with milk consumption and a higher level of BCM-7. Therefore, careful attention should be paid to that protein polymorphism, and deeper research is needed to verify the range and nature of its interactions with the human gastrointestinal tract and whole organism.

[URL til studie]

Bioactive Milk Peptides: A Prospectus
D. A. Clare* and H. E. Swaisgood †
*Department of Food Science †Departments of Food Science and Biochemistry
North Carolina State University

Bioactive peptides have been identified within the amino acid sequences of native milk proteins. Hydrolytic reactions, such as those catalyzed by digestive enzymes, result in their release. These peptides directly influence numerous biological processes evoking behavioral, gastrointestinal, hormonal, immunological, neurological, and nutritional responses. The specific bioreactions associated with each physiological class have been well characterized.

Herein, we review the scientific literature and attempt to stimulate consideration of the continued use of bioactive peptides and their expanded development as a commercial product. Several applications have already evolved. For example, phosphopeptides derived from casein fractions are currently used as both dietary and pharmaceutical supplements. Potentially, the addition of bioactive peptides to food products could improve consumer safety as a result of their antimicrobial properties.

Lastly, bioactive peptides may function as health care products, providing therapeutic value for either treatment of infection or prevention of disease.
[Url til artikkel]

Curr Pharm Des. 2003;9(16):1325-30.Links
Delta opioid peptides derived from plant proteins.
Yoshikawa M, Takahashi M, Yang S.
Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Kyoto 611-0011, Japan. Denne e-postadressen er beskyttet mot programmer som samler e-postadresser. Du må aktivere javaskript for å kunne se den.

Opioid peptides showing selectivity for delta receptor have been isolated from enzymatic digests of plant proteins. Five peptides were derived from wheat gluten, and named gluten exorphins A5, A4, B5, B4 and C. Two opioid peptides were also released from spinach ribulose-bisphosphate-carboxylase/oxygenase (Rubisco), and named rubiscolins-5 and -6. Among them, gluten exorphin 5A (Gly-Tyr-Tyr-Pro-Thr) and rubiscolin 6 (Tyr-Pro-Leu-Asp-leu-Phe) improved learning performance in step-through type passive avoidance test after post-training oral administration in mice at doses of 300 mg/kg and 100 mg/kg, respectively, which are smaller than those required for antinociceptive activity.

PMID: 12769740 [PubMed - indexed for MEDLINE]

Opioid peptides encrypted in intact milk protein sequences
Hans Meisela and R. J. FitzGeralda -  British Journal of Nutrition (2000)

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.
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