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

ABSTRACT: This work systematically investigated the dose-response interaction between hydroxy-α-sanshool (α-SOH) and pork myofibrillar proteins (MPs) via spectroscopy, molecular docking, and molecular dynamics simulation methods. Results showed that MPs bound with low α-SOH can enhance the surface hydrophobicity and particle size of MPs, whereas high concentrations were exactly the opposite. The main interaction force in α-SOH/MPs complex changed from hydrophobic to hydrogen bonding with increased α-SOH. α-SOH causes tryptophan quenching and bring about a red shift at low concentration, as well as to promote α-helix conversion into β-sheet in MPs. Simultaneously, molecular docking and dynamics simulations verified that hydrogen bonding and hydr

SUBMITTER: Zhao J 

PROVIDER: S-EPMC10740131 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature