Integration of Molecular Docking Analysis and Molecular Dynamics Simulations for Studying Food Proteins and Bioactive Peptides

In silico tools, such as molecular docking, are widely applied to study interactions and binding affinity of biological activity of proteins and peptides. However, restricted sampling of both ligand and receptor conformations and use of approximated scoring functions can produce results that do not correlate with actual experimental binding affinities. Molecular dynamics simulations (MDS) can provide valuable information in deciphering functional mechanisms of proteins/peptides and other biomolecules, overcoming the rigid sampling limitations in docking analysis. This review will discuss the information related to the traditional use of in silico models, such as molecular docking, and its application for studying food proteins and bioactive peptides, followed by an in-depth introduction to the theory of MDS and description of why these molecular simulation techniques are important in the theoretical prediction of structural and functional dynamics of food proteins and bioactive peptides. Applications, limitations, and future prospects of MDS will also be discussed.

Automated summary

The use of in silico tools, such as molecular docking, to study biological activity of proteins and peptides can sometimes produce results that do not correlate with actual experimental binding affinities. Molecular dynamics simulations (MDS) offer a solution to overcome sampling limitations in docking analysis and provide valuable information in deciphering functional mechanisms of proteins and peptides. This review discusses the traditional use of in silico models, like molecular docking, and highlights the importance of MDS in predicting structural and functional dynamics of food proteins and bioactive peptides.