Exploring the taste presentation and receptor perception mechanism of salty peptides from <em>Stropharia rugosoannulata</em> based on molecular dynamics and thermodynamics simulation

The taste presentation and receptor perception mechanism of the salty peptide Stropharia rugosoannulata were predicted verified using omics molecular interaction techniques. combination aspartic acid (D) glutamic (E), or fragments composed arginine (R), constitute characteristic structural basis peptides S. rugosoannulata. intensity positively correlates with its concentration within a specific range ((0.25-1.0) mg/mL). more easily recognizes first amino residue at N-terminal in peptides. GLU513, ASP707, VAL508 are critical residues for to recognize TRPV1 is specifically recognizing Hydrogen bonds electrostatic interactions main driving forces between receptors. KSWDDFFTR has most potent binding capacity tremendous potential application sodium salt substitution. This study confirmed that peptides, analyzed receptor-peptide interaction, provided new idea understanding