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Synthesis, characterization, and sweetness‐suppressing activities of gurmarin analogues missing one disulfide bond
Author(s) -
Ota Masafumi,
Shimizu Yasutake,
Tonosaki Keiichi,
Ariyoshi Yasuo
Publication year - 1998
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(199808)46:2<65::aid-bip2>3.0.co;2-v
Subject(s) - chemistry , protein disulfide isomerase , sweetness , disulfide bond , stereochemistry , alanine , intramolecular force , glycine , amino acid , biochemistry , sugar
The sweetness‐suppressing polypeptide gurmarin isolated from Gymnema sylvestre consists of 35 amino acid residues and includes three intramolecular disulfide bonds. The roles of the three disulfide bonds were investigated by replacing each with two alanine residues by solid‐phase synthesis. Nine analogues of [Ala 3,18 ]gurmarin, [Ala 10,23 ]gurmarin, and [Ala 17,33 ]‐gurmarin were obtained. Three analogues had native disulfide bonds, while the other six had non‐native disulfide bonds. The three analogues with native disulfide bonds suppressed the response to sucrose, but not those to glucose, fructose, saccharin, or glycine in rats. In contrast, the six analogues with non‐native disulfide bonds did not suppress the responses to any of these sweeteners. These results suggest that the native disulfide bonds of gurmarin are necessary for interaction with the receptor protein, and that the sucrose‐specific receptor site is present in rats. © 1998 John Wiley & Sons, Inc. Biopoly 46: 65–73, 1998