Taste mechanism of kokumi peptides from yeast extracts revealed by molecular docking and molecular dynamics simulation
Jincui Chang, Tao Feng, Haining Zhuang, Shiqing Song, Min Sun, Lingyun Yao +6 more
Journal of Future Foods
Abstract
Peptides have been used as flavors for decades, however, their tasting mechanism remains not entirely clear. In the present work, 10 kokumi peptides identified in yeast extracts were selected as ligands. Their binding mechanism to calcium-sensitive receptors (CaSR) were investigated at molecular level by using molecular docking and molecular dynamics simulations. The results showed that all kokumi peptides could bind to CaSR to form complexes, of which γ-Glu-Cys-Gly (GSH), γ-Glu-Leu (EL) and γ-Glu-Tyr (EY) being the top 3 peptides with higher affinity. Arg66, Ser147 and Ala168 may be the active sites of CaSR and interact with CaSR through hydrogen bonds; the different kokumi peptides and CaSR mainly rely on hydrogen bonding, electrostatic interaction and hydrophobic interaction to bind each other. This study provides a theoretical reference for the interaction between kokumi peptides and their receptors.
Extracted Claims
4 claims extracted from this paper into the knowledge graph
kokumi peptides and CaSR interact through hydrogen bonds, electrostatic interaction, and hydrophobic interaction
“the different kokumi peptides and CaSR mainly rely on hydrogen bonding, electrostatic interaction and hydrophobic interaction to bind each other”
Arg66, Ser147, and Ala168 may be the active sites of CaSR
“Arg66, Ser147 and Ala168 may be the active sites of CaSR”
kokumi peptides bind to calcium-sensitive receptors (CaSR)
“all kokumi peptides could bind to CaSR to form complexes”