Unravelling the interaction between α-SOH and myofibrillar protein based on spectroscopy and molecular dynamics simulation

This work systematically investigated the dose-response interaction between hydroxy-alpha-sanshool (alpha-SOH) and pork myofibrillar proteins (MPs) via spectroscopy, molecular docking, and molecular dynamics simulation methods. Results showed that MPs bound with low alpha-SOH can enhance the surface hydrophobicity and particle size of MPs, whereas high concentrations were exactly the opposite. The main interaction force in alpha-SOH/MPs complex changed from hydrophobic to hydrogen bonding with increased alpha-SOH. alpha-SOH causes tryptophan quenching and bring about a red shift at low concentration, as well as to promote alpha-helix conversion into beta-sheet in MPs. Simultaneously, molecular docking and dynamics simulations verified that hydrogen bonding and hydrophobic forces were the main contributors to alpha-SOH/MPs complex, indicating that the binding of alpha-SOH with MPs proceeded spontaneously with high intensity, in which TYR286 contributed the most significant energy. Therefore, revealing the binding mechanism of alpha-SOH and MPs can contribute to the deep processing of numbing meat products.