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 A3 to 1135.75 A3. 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.