The research aimed to elucidate the interaction and mechanism between the Portulaca oleracea L. extract (POE) and the pork myofibrillar proteins (MPs) from the perspectives of fluorescence spectroscopy and molecular docking. The results showed that POE significantly increased intermolecular hydrogen bonds and hydrophobic interactions in MPs (P 0, and ∆S > 0 indicated that the binding process between POE and MPs was spontaneous, with hydrophobic interactions being the primary driving force. Additionally, the nine most abundant compounds in POE were selected for molecular docking with myosin, and the binding energies were all negative, confirming that POE could spontaneously interact with MPs. The molecular docking results further demonstrated that hydrophobic interactions and hydrogen bonding were the main binding forces, with Leu270 potentially serving as a key amino acid residue in the interaction between POE and MPs. This study provides valuable insights into the molecular interactions between Portulaca oleracea L. extract and pork myofibrillar proteins, offering a theoretical basis for phenolic small molecule substances in regulating protein oxidation and potential applications in improving meat product quality.
Chang et al. (Sun,) studied this question.