Identification of novel umami peptides from myosin via homology modeling and molecular docking

Abstract

The structure of the umami receptor T1R1/T1R3 was constructed using homology modeling and molecular dynamics, and the interactions between peptides and this umami receptor were studied by molecular docking. The umami intensity of the peptides was also investigated by using an electronic tongue. The results showed that 99.3% of the amino acid residues in the homologous model of the T1R1/T1R3 heterodimer were within the allowable range, which is greater than the threshold requirement of 90% of the residues in the high-quality model structure. Five novel peptides (DK, EEK, EDQK, SEGGR, and QDSIGS) were selected and synthesized. The umami intensity of these five peptides was stronger than that of monosodium glutamate. The docking results revealed that the interactions between peptides and the major amino acids residues Arg151, Asp147, and Gln52 of T1R1 play critical roles in the production of umami taste.