Abstract：
This study examined the interaction between myofibrillar proteins (MPs) and the numbing substance hydroxy-α-sanshool (α-SOH) in a thermal environment, and provided an explanation of the numbness perception mechanism through muti-spectroscopic and molecular dynamics simulation methodology. Results showed that addition of α-SOH could reduce the particle size and molecular weight of MPs, accompanied by changes in the tertiary and secondary structure, causing the α-helix of MPs transitioned to β-sheet and β-turn due to the reorganization of hydrogen bonds. After a moderate heating (60 or 70 °C), MPs could form the stable complexes with α-SOH that were associated with attachment sites and protein wrapping. The thermal process might convert a portion of α-SOH\' into hydroxy-β-sanshool\' (β-SOH\'). When docking with the sensory receptor TRPV1, the RMSD, RMSF and binding free energy all showed that β-SOH\' demonstrated a low affinity, thereby reducing the numbing perception. These findings can provide a theoretical foundation for the advanced processing of numbing meat products.
摘要：
这项研究检查了热环境中肌原纤维蛋白（MPs）与麻木物质羟基-α-sanshool（α-SOH）之间的相互作用，并通过多光谱和分子动力学模拟方法解释了麻木感知机制。结果表明,α-SOH的加入可以降低MPs的粒径和分子量,伴随着三级和二级结构的变化，由于氢键的重组，导致MP的α螺旋过渡到β折叠和β转角。经过适度加热（60或70°C），MPs可以与α-SOH形成稳定的复合物，这些复合物与附着位点和蛋白质包裹有关。热过程可能会将一部分α-SOH转化为羟基-β-sanshool'（β-SOH'）。当与感觉受体TRPV1对接时，RMSD，RMSF和结合自由能都表明β-SOH表现出低亲和力，从而减少麻木的感觉。这些发现可为麻木肉制品的深加工提供理论依据。
