Abstract
The study of ligand-receptor interactions is of great significance in food flavor perception. In this study, a computer simulation method was used to investigate the mechanism of interaction between umami peptides and T1R1/T1R3-VFT receptor. The binding site, conformational changes, and binding free energy between umami peptides and T1R1/T1R3-VFT were analyzed through molecular modeling, molecular docking, and molecular dynamics simulations. The receptor model constructed using AlphaFold2 has the best rationality. The molecular docking results showed that umami peptides primarily bound to T1R1-VFT through hydrogen bonding, with key binding residues such as 149THR, 151ARG, and 108ASP. The binding of umami peptides led to a more stable complex system, and the positively charged amino acids contributed positively to the overall binding free energy. This study provides theoretical support for the development of a better understanding of the interaction between umami substances and the umami receptor.
