Department of Physics, Indian Institute of Technology (Indian School of Mines), Dhanbad, Jharkhand, India.
J Biomol Struct Dyn. 2022 Mar;40(5):2146-2155. doi: 10.1080/07391102.2020.1835731. Epub 2020 Oct 19.
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.
β-乳球蛋白（βLG）是一种主要的乳清蛋白，具有结合各种配体的潜力；因此，它被用作蛋白质-配体相互作用研究的模型蛋白。维生素 B12 是人体必需的营养物质，有助于 DNA、蛋白质的合成和红细胞的生成。维生素 B12 与 βLG 的结合相互作用将有助于了解 βLG 作为维生素 B12 载体的效力。我们的实验结果已经表明，βLG 成功地与维生素 B12 结合（Swain 等人，2020 年）。然而，为了更有力地支持我们的实验结果，在这里，我们使用了计算工具，如分子对接和分子动力学（MD）模拟。分子对接技术用于阐明维生素 B12 在 βLG 上的可能结合位点和结合亲和力。对维生素 B12 与 βLG 的对接复合物进行了 MD 模拟，以研究其在一段时间内的稳定性和其他相互作用特性。研究表明，该化合物是稳定的，维生素 B12 不会改变 βLG 的二级结构。计算结果与我们的实验研究相当吻合。
