Insights into the interactions between etheric compounds and myofibrillar proteins using multi-spectroscopy, molecular docking, and molecular dynamics simulation

This study aimed to examine how the addition of etheric compounds (EC) affects the characteristics of myofibrillar proteins (MP) and to understand underlying interaction mechanisms. Fourier transform infrared spectroscopy confirmed that the EC-MP complex was formed through hydrogen bonding. The addition of EC resulted in an increase in the α-helix content and a decrease in the β-sheet content of MP, which would promote the protein unfolding. The unfolding of MP led to aggregation and formation of larger and non-uniform particles. As a result, the exposure of negative charge on the MP surface was enhanced, and zeta potential was decreased from -5.33 mV to -7.45 mV. Moreover, the EC-induced modification of MP conformation resulted in a less rigid three-dimensional network structure of MP gel and enhanced the discharge of aldehyde compounds (C > 6). Moreover, the rheological characteristics of MP were enhanced by the suppression of protein-protein interactions due to the MP unfolding. Molecular dynamics simulations revealed that anethole reduced the binding capacity of myosin to decanal by raising its binding energy from -22.22 kcal/mol to -19.38 kcal/mol. In the meantime, anethole competed for the amino acid residue (PHE165) where myosin connects to decanal. This caused the hydrogen bonds and hydrophobic contacts between the two molecules to dissolve, altering myosin's conformation and releasing decanal. The results might be useful in predicting and controlling the ability of proteins to release and hold onto flavors.