Molecular Docking and Simulation of the Synergistic Effect Between Umami Peptides, Monosodium Glutamate and Taste Receptor T1R1/T1R3

In order to investigate the synergistic effect between umami peptides, monosodium glutamate (MSG) and the taste receptor T1R1/T1R3, a novel bivariate model was created based on our previous work. The results showed three specific changes upon the addition of MSG between umami peptides and T1R1/T1R3, in terms of energy and conformation. First, the addition of MSG enlarged the size of the binding cavity of T1R3 from 534.125 A to 1135.75 A. Second, the addition of MSG caused small peptides to bind with T1R3, with the lowest docking energy and docking interaction energy, -77.2295 and -60.7146 kcal/mol respectively. Third, five binding residues ,including Glu-429, Gln-302, Gly-304, Try-107 and His-364, increased which play critical roles in hydrogen bonding. They are consistent with the results of electronic tongue and facilitate better understanding of the synergism. Furthermore, novel umami and umami-enhanced compounds could be discovered, based on the use of the novel bivariate model.