Elucidating the binding mechanism of silver carp myosin to T-2 toxin using multi-spectroscopic analysis, molecular docking and molecular dynamics simulation

Mycotoxin contamination is a potential hazard to aquatic product processing industry. T-2 toxin, mycotoxin produced by Fusarium , significantly affects the muscle structure of aquatic animal, resulting in reduced muscle quality and compromised food safety. The interaction mechanism between silver carp myosin and T-2 toxin was investigated using multi-spectroscopic analysis, molecular docking and molecular dynamics (MD) simulation methods. T-2 toxin binds to myosin through hydrophobic interaction, altering its secondary structure, by decreasing the α-helix content and increasing the β-sheet and β-turn formations, as revealed by circular dichroism analysis. UV– vis and fluorescence spectra revealed that T-2 toxin induced a reduction in the total sulfhydryl content and surface hydrophobicity of myosin. Furthermore, molecular docking indicated that T-2 entered the hydrophobic active pocket of myosin and formed a hydrogen bond with Thr-80 and Tyr-247. MD simulation confirmed that T-2 altered the actin-myosin structure, lead to increased fluctuations in root mean square deviation and radius of gyration values of the resulting complex-formed. Following the binding of T-2 to actin-myosin, the rigidity of amino acid residues at junction position and the structure compactness of myofibrillar proteins were reduced. This study highlights the interaction between T-2 toxin and muscle tissue, providing valuable insights for monitoring and control of mycotoxin contamination. • T-2 toxin binds to silver carp myosin, altering its secondary structure and function. • Circular dichroism showed decreased α-helix and increased β-sheet content. • UV– vis and fluorescence indicated reduced sulfhydryl content in myosin. • Molecular docking revealed that T-2 binds within myosin's hydrophobic pocket. • MD simulation showed increased fluctuations in myofibrillar protein structure.