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.
摘要:
这项工作通过光谱学系统地研究了羟基-α-sanshool(α-SOH)与猪肉肌原纤维蛋白(MPs)之间的剂量反应相互作用,分子对接,分子动力学模拟方法。结果表明,与低α-SOH结合的MPs可以增强MPs的表面疏水性和粒径,而高浓度正好相反。随着α-SOH的增加,α-SOH/MPs复合物中的主要相互作用力从疏水变为氢键。α-SOH引起色氨酸猝灭并在低浓度下引起红移,以及促进MPs中α-螺旋转化为β-折叠。同时,分子对接和动力学模拟验证了氢键和疏水性力是α-SOH/MPs复合物的主要贡献者,表明α-SOH与MPs的结合以高强度自发进行,其中TYR286贡献了最显著的能量。因此,揭示α-SOH与MPs的结合机制有助于麻木肉制品的深加工。