Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Food & Nutrition Science Communications
Soymorphins, Novel μ Opioid Peptides Derived from Soy β-Conglycinin β-Subunit, Have Anxiolytic Activities
Kousaku OHINATAShun AGUIMasaaki YOSHIKAWA
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JOURNAL FREE ACCESS

2007 Volume 71 Issue 10 Pages 2618-2621

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Abstract

Based on the amino acid sequence YPFV found in the soy β-conglycinin β-subunit, which is common to an opioid peptide human β-casomorphin-4, peptides YPFVV, YPFVVN, and YPFVVNA were synthesized according to their primary structure. On guinea pig ileum (GPI) assay, they showed opioid activity (IC50 = 6.0, 9.2 and 13 μM respectively) more potent than human β-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 μ opioid receptor. Human β-casomorphin-4 and soymorphin-5 were released from the soy 7S fraction (β-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.

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© 2007 by Japan Society for Bioscience, Biotechnology, and Agrochemistry
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