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Opioid peptides derived from wheat gluten: Their isolation and characterization
Author(s) -
Fukudome Shin-ichi,
Yoshikawa Masaaki
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80414-c
Subject(s) - glutenin , gluten , chemistry , wheat gluten , peptide , biochemistry , opioid peptide , receptor , enzyme , opioid , gene , protein subunit
Four opioid peptides were isolated from the enzymatic digest of wheat gluten. Their structures were Gly‐Tyr‐Tyr‐Pro‐Thr, Gly‐Tyr‐Tyr‐Pro,Tyr‐Gly‐Gly‐Trp‐Leu and Tyr‐Gly‐Gly‐Trp, which were named gluten exorphins A5, A4, B5 and B4, respectively. The gluten exorphin A5 sequence was found at 15 sites in the primary structure of the high molecular weight glutenin and was highly specific for δ‐receptors. The structure—activity relationships of gluten exorphins A were unique in that the presence of Gly at their N‐termini increased their activities. Gluten exorphin B5, which corresponds to [Trp 4 ,Leu 5 ]enkephalin, showed the most potent activity among these peptides. Its IC 50 values were 0.05 μM and 0.017 μM, respectively, on the GPI and the MVD assays.