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

• Published in: Food Chemistry: X 2023-12, Vol.20, p.100986-100986, Article 100986
• Main Authors: Zhao, Jie, Wang, Shuaiqian, Jiang, Diandian, Lu, Yan, Chen, Yu, Tang, Yong, Tang, Jie, Jiang, Zhenju, Lin, Hongbin, Dong, Wei
• Format: Article
• Language: English
• Subjects: Hydroxy-α-sanshool; Interaction mechanism; Molecular dynamics simulation; Myofibrillar proteins; Spectroscopy
• ISSN: 2590-1575; 2590-1575
• DOI: 10.1016/j.fochx.2023.100986

[Display omitted] •α-SOH reduced the fluorescence of MPs by combining quenching.•The binding of α-SOH to MPs promoted α-helix convert into β-sheet in MPs.•Myosin TYR286 amino acid residue has the lowest binding energy to α-SOH. 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 hydrophobic forces were the main contributors to α-SOH/MPs complex, indicating that the binding of α-SOH with MPs proceeded spontaneously with high intensity, in which TYR286 contributed the most significant energy. Therefore, revealing the binding mechanism of α-SOH and MPs can contribute to the deep processing of numbing meat products.