Probing the mechanism of interaction between capsaicin and myofibrillar proteins through multispectral, molecular docking, and molecular dynamics simulation methods

The interaction between myofibrillar proteins (MPs) and capsaicin (CAP) was investigated using multispectral, molecular docking, and molecular dynamics simulation methods. The resulting complex increased the hydrophobicity of the tryptophan and tyrosine microenvironment as revealed by fluorescence spectral analysis. The fluorescence burst mechanism study indicated that the fluorescence burst of CAP on the MPs was a static one (Kq = 1.386 x 1012 m-1s  1) and that CAP could bind with MPs well (Ka = 3.31 x 104 L/mol, n = 1.09). The analysis of circular dichroism demonstrated that the interaction between CAP and MPs caused a decrease in the & alpha;-helical structure of MPs. The complexes formed exhibited lower particle size and higher absolute & zeta; potential. Furthermore, hydrogen bonding, van der Waals forces, and hydrophobic interactions were found to be the primary factors facilitating the interaction between CAP and MPs, as suggested by molecular docking models and molecular dynamics simulations.

Automated summary

The interaction between myofibrillar proteins (MPs) and capsaicin (CAP) was investigated using multispectral, molecular docking, and molecular dynamics simulation methods. The study found that the resulting complex increased the hydrophobicity of the tryptophan and tyrosine microenvironment as revealed by fluorescence spectral analysis. It was also discovered that the interaction between CAP and MPs was primarily facilitated by hydrogen bonding, van der Waals forces, and hydrophobic interactions, as suggested by molecular docking models and molecular dynamics simulations.