Integrated experiments and molecular dynamics simulation to decipher the interaction of marine phospholipids with myosin: Focus on binding mechanisms, conformation, and functional properties.

Marine phospholipids enhance the quality of meat products, but the fundamental mechanism remains unclear. This study aimed to decipher the binding and interaction mechanisms of the main component of marine phospholipids, docosahexaenoic acid-containing phosphatidylcholine (PC-DHA), with functional protein (myosin) of meat products by multi-spectroscopy and molecular dynamics simulations (MDS). Furthermore, this study experimentally analyzed the functional properties of myosin-PC-DHA complex. The spectroscopy showed that PC-DHA interacted with myosin through static quenching to form a stable complex. MDS demonstrated that PC-DHA induced conformational changes in myosin by altering the strength and direction of movement of key amino acid residues. Moreover, MDS revealed that the interaction with PC-DHA increased the solvent contact area and irregularly curled structure of myosin, giving myosin a higher solvent-accessible surface area and more contact sites. These structural changes promoted improved gelling and emulsifying properties of myosin. This study provides a theoretical framework for an in-depth understanding of the mechanisms by which marine phospholipids regulate the quality of meat foods.