In-depth investigation of the interaction between quercetin and myoglobin: A combined spectroscopy, molecular docking, and molecular dynamics simulation approach

Myoglobin is a key factor affecting meat color. Previous studies have been carried out on quercetin in regulating the redox state of myoglobin and retaining meat color. Based on this, multi-spectroscopic analysis combined with molecular docking and molecular dynamics simulation, were used to explore the interaction between quercetin and myoglobin. The results showed that the interaction between quercetin and myoglobin was mainly driven by van der Waals force and hydrogen bond, and the process was a spontaneous exothermic reaction. This interaction changed the inherent structure of myoglobin, improved its antioxidant activity and thermal stability, and reduced surface hydrophobicity and solubility. In this study, the interaction mechanism between quercetin and myoglobin was elucidated in detail from the molecular level, which may provide a strong scientific information for the use of quercetin in meat processing to maintain meat color stability and develop high-quality and attractive meat products. • Quercetin plays a role in protecting meat color by interacting with myoglobin. • The interaction between quercetin and myoglobin is mainly through van der Waals forces and hydrogen bonds. • Quercetin-myoglobin complexes changed the secondary structure of myoglobin. • Non-covalent interactions improved the antioxidant activity and thermal stability of myoglobin.