Identification and molecular mechanism of novel salt-enhancing peptide in crocodile hemoglobin: a combined E-tongue, molecular docking, and dynamic simulation.

BACKGROUND

This study aimed to reduce salt intake without compromising food sensory properties. Novel salt-enhancing peptides were identified from crocodile hemoglobin via virtual screening and evaluated for their salt-reducing effects using molecular docking, electronic tongue analysis, and molecular dynamics simulations.

RESULTS

A total of 24 water-soluble and non-toxic peptides were obtained by virtual enzymolysis. The protein structure of human transmembrane channel-like 4 (TMC4), a novel salt taste receptor, was constructed using AlphaFold2 and applied as a receptor. The salt-reducing effect of these peptides was verified using electronic tongue analysis, in which the peptide SSDDK had a significant salt-reducing effect. Molecular docking results showed that the main force for peptide binding to the TMC4 receptor was conventional hydrogen bonding, and Arg 583, Arg330, and Glu284 were the key amino acid residues for its binding. Molecular dynamics simulations also verified the stability of peptide-receptor binding.

CONCLUSION

This study demonstrates that the peptide SSDDK, derived from crocodile hemoglobin, can be used to enhance salty taste and reduce sodium salt use. © 2025 Society of Chemical Industry.