Understanding interactions among aldehyde compounds and porcine myofibrillar proteins by spectroscopy and molecular dynamics simulations

Interactions among four aldehydes (3-methyl butanal, pentanal, hexanal, and heptanal) and myofibrillar proteins (MPs) were investigated in this study. Overall, the results and analyses demonstrate that the binding capacities of the aldehydes were substantially enhanced as protein concentration increased (p < 0.05). Moreover, aldehydes with longer carbon chains exhibited stronger protein binding (p < 0.05). Interactions between MPs and aldehyde species can occur through irreversible covalent binding and reversible physicochemical binding, with covalent binding likely playing a more dominant role. Static quenching was observed during MPs-heptanal binding experiments, which led to changes in the secondary structure and micro-environment of the MPs. Complementary molecular docking/dynamic simulations further established that hydrophobic interactions were the major driving force for reversible binding of the aldehyde species and contributed to the stability of the myosin-heptanal system. This study provides molecular-level insights into the mechanism of the interaction between aldehydes and MPs.