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

Jie Zhao; Shuaiqian Wang; Diandian Jiang; Yan Lu; Yu Chen; Yong Tang; Jie Tang; Zhenju Jiang; Hongbin Lin; Wei Dong

doi:10.1016/j.fochx.2023.100986

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

Food Chem X. 2023 Nov 8:20:100986. doi: 10.1016/j.fochx.2023.100986. eCollection 2023 Dec 30.

Authors

Jie Zhao^{1

2}, Shuaiqian Wang¹, Diandian Jiang¹, Yan Lu¹, Yu Chen¹, Yong Tang^{1

2}, Jie Tang^{1

2}, Zhenju Jiang^{1

2}, Hongbin Lin^{1

2}, Wei Dong³

Affiliations

¹ School of Food and Bioengineering, Xihua University, Chengdu 610039, China.
² Chongqing Key Laboratory of Speciality Food Co-Built by Sichuan and Chongqing, Chengdu 610039, China.
³ Beijing Laboratory of Food Quality and Safety/Key Laboratory of Alcoholic Beverages Quality and Safety of China Light Industry, Beijing Technology and Business University, Beijing 100048, China.

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 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.

Keywords: Hydroxy-α-sanshool; Interaction mechanism; Molecular dynamics simulation; Myofibrillar proteins; Spectroscopy.