Molecular dynamics simulation of the interactions between sesamol and myosin combined with spectroscopy and molecular docking studies

In this study, the mechanism of the interactions between sesamol and myosin was explored to confirm the potential application of sesamol in a meat protein system. A series of sesamol and myosin solutions were prepared for spectroscopic studies. UV-vis spectroscopy revealed that sesamol formed a complex with myosin and affected the myosin microenvironment. Fourier transform infrared spectroscopy showed that hydrogen bonding was involved in the formation of the complex. Static quenching (Kq = 1.044 x 10(12) m(-1) s(-1)) of sesamol on myosin and the good binding effect (Ka = 1.44 x 10(5) L/mol, n = 1.33) between sesamol and myosin were verified by the fluorescence quenching mechanism. Circular dichroism spectroscopy confirmed that the interactions resulted in a decrease of myosin a-helix content. Furthermore, the best pose for successfully docking sesamol with myosin (lowest binding affinity of -6.2 kcal/mol) was shown by molecular docking. The molecular dynamics simulation and small-angle X-ray scattering results determined that hydrophobic interactions and hydrogen bonding allowed the protein structure to be more compact and stabilized. Several key residues (Glu-477, Cys-480, Ile-481, Glu-272, Leu-271, and Leu-270) and a protein residue (Lys-273) formed a structurally stable complex with sesamol through hydrophobic interactions and hydrogen bonding (3.28 A). The surface hydrophobicity of the sesamol-myosin complex was reduced, solubility and emulsification properties were improved, and a smaller particle size was produced.