The effects of the L-hisdine (L-His)-assisted ultrasound on physicochemical characteristics and conformation of myofibrillar protein (MP) under reduced-salt condition were investigated using spectroscopic analysis, and the binding mechanism between L-His and MP was further elucidated through molecular docking and molecular dynamics (MD) simulations. UV second derivative spectra and intrinsic Try fluorescence spectra revealed that L-His formed a complex with MP and altered the microenvironment of MP. After L-His-assisted ultrasound treatment, MP showed smaller particle size, higher solubility, and more uniform atomic force microscopy image due to the decrease of α-helix content and the subsequent increase in zeta potential, active sulfhydryl content, and surface hydrophobicity. Molecular docking and MD simulations demonstrated the optimal docking pose (minimum binding affinity of -6.78 kcal/mol) and revealed hydrophobic interactions and hydrogen bonds as the main interaction forces between L-His and MP, with several residues (ILE-464, ILE-480, THR-483, ASN-484, GLY-466, ASP-463, PHE-246) identified as binding sites.
Keywords: L-hisdine; Low-salt condition; Molecular dynamics simulations; Myofibrillar protein; Spectroscopic analysis; Ultrasound.
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