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The β-Lactoglobulin (βLG) is a major whey protein that has the potential to bind various ligands; hence it is used as a model protein in protein-ligand interaction studies. Vitamin B12 is an essential nutrient for the human body, which helps in the synthesis of DNA, proteins, and the production of red blood cells. Binding interaction of vitamin B12 with βLG will help to understand the potency of βLG as a transporter for vitamin B12. Our experimental findings already showed that βLG binds with vitamin B12 successfully (Swain et al.,  2020 ). Nevertheless, to further support our experimental results firmly, here, we have employed computational tools such as molecular docking and molecular dynamics (MD) simulation. The molecular docking technique was used to elucidate the probable binding sites and binding affinity of vitamin B12 on βLG. The docked complex of vitamin B12 with βLG was subjected to MD simulation to investigate its stability and other interaction properties over a time frame. The study revealed that the compound is stable, and vitamin B12 imposes no change to the secondary structure of the βLG. The computational results agree reasonably well with our experimental study.

Interaction of vitamin B12 with β-lactoglobulin: a computational study