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Conformational flexibility of aspartame
Author(s) -
Toniolo Claudio,
Temussi Pierandrea
Publication year - 2016
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22847
Subject(s) - aspartame , dipeptide , chemistry , sweet taste , phenylalanine , artificial sweetener , docking (animal) , stereochemistry , homology modeling , flexibility (engineering) , taste , biochemistry , sugar , amino acid , enzyme , medicine , nursing , statistics , mathematics
ABSTRACT L‐Aspartyl‐L‐phenylalanine methyl ester, better known as aspartame, is not only one of the most used artificial sweeteners, but also a very interesting molecule with respect to the correlation between molecular structure and taste. The extreme conformational flexibility of this dipeptide posed a huge difficulty when researchers tried to use it as a lead compound to design new sweeteners. In particular, it was difficult to take advantage of its molecular model as a mold to infer the shape of the, then unknown, active site of the sweet taste receptor. Here, we follow the story of the 3D structural aspects of aspartame from early conformational studies to recent docking into homology models of the receptor. © 2016 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 106: 376–384, 2016.