Exploring the characteristics and mechanisms of novel salt taste-enhancing peptides from porcine bone collagen via virtual screening, sensory evaluation, and molecular dynamics simulations.

This study aimed to identify salt taste-enhancing peptides from porcine bone collagen. In silico hydrolysis coupled with virtual screening identified eight potential salt taste-enhancing peptides. Further validation using sensory evaluation and electronic tongue analysis demonstrated that peptides DGGR, GAPGDR, VGPRGERGF, PGQRGERGF, and EMATQLAFMR enhanced the saltiness perception of a 0.3 % NaCl solution. Among these, DGGR exhibited the strongest salt taste-enhancing effect. DGGR, GAPGDR, VGPRGERGF, and EMATQLAFMR exhibited synergistic effects with NaCl, while PGQRGERGF showed an additive effect. Molecular docking studies revealed that these peptides interact primarily with the TMC4 receptor through hydrogen bonds and van der Waals forces, with Arg130, Arg330, Glu319, Glu326, and Thr581 identified as key sites. Molecular dynamics simulations further confirmed that these peptides form stable complexes with the TMC4 receptor through strong hydrogen bond interactions. This research not only enhanced the utilization of porcine by-products, but also contributed to the development of novel salt taste enhancers.