Hydroxy-α-sanshool (α-SOH)， an amide in peppercorns， interacts with proteins to enhance the numbness of meat dishes in Sichuan cuisine. In order to clarify the structural changes and attachment of the two in meat processing， this experiment explored the mechanism of heat-induced (60， 70， 90 ℃) interactions between pork myofibrillar proteins (MPs) and α-SOH， and resolved the mechanism of numbness activation of α-SOH by molecular docking. The results showed that α-SOH increases the surface hydrophobicity of α-SOH/MPs complexes and promotes the depolymerization of heat-treated MPs. Moreover， the N-H bond in the amide group of α-SOH readily formed stabilizing hydrogen bonds between amino acid residues and altered the subunit aggregation state of the protein， thereby significantly attenuating the bands larger than 45 ku on SDS-PAGE. Fluorescence mapping and circular dichroism results confirmed that α-SOH leads to the transition of protein secondary structure from a regular to a disordered state. Moderately heat-treated (60 ℃ and 70 ℃) MPs were more likely to form complexes with α-SOH， thus reducing the free α-SOH content. The molecular docking results showed that α-SOH activation of hemp flavor was produced by binding to L681 on the TRPV1 receptor. This experiment elucidates the mechanism of interaction between MPs and α-SOH as well as the mechanism of activation of numbness， which can provide a theoretical basis for the regulation of numbness in the processing of meat products.