The structure features of umami hexapeptides for the T1R1/T1R3 receptor

- Night peptides from hydrolyzed muscle of Takifugu obscurus was identified.
- Umami hexapeptides was used to build a (3D-QSAR) model successfully.
- The structure-activity of umami hexapeptides were preliminary illustrated.

Umami is thought to be initiated by binding tastants to G-protein-coupled receptors in taste cells, while the structure and mechanism of the receptors are not clear. In this study, we summarized umami peptides and classified them roughly into two groups: the first group contains dipeptides and tripeptides with terminal Glu or Asp, while the second peptides comprises more amino acids without significant features. The research on the structure and taste characteristics of second group peptides are less studied, so we focus on this group. In this work, nine flavor peptides were newly identified from Takifugu obscurus, and among them, the umami hexapeptides KGRYER belong to the second group. Five hexapeptides from this study, our previous work and references were chosen to build a Three Dimensional Quantitative Structure-Activity Relationship model with q2 value as 0.964 successfully. Then the relationship between the structure and intensity of umami peptides were illustrated.