East European Journal of Physics, Journal Year: 2024, Volume and Issue: 4, P. 511 - 517

Published: Dec. 8, 2024

β-Lactoglobulin (β-lg), the predominant whey protein, is renowned for its nutritional and functional attributes, including ability to bind hydrophobic charged molecules. These properties make β-lg a promising candidate applications such as drug delivery systems, nutraceutical carriers, nanocomposites environmental remediation, particularly in detecting removing heavy metals. Despite potential, impact of metal binding on β-lg's structure stability remains insufficiently explored, posing challenges advanced applications. In this study, molecular dynamics (MD) simulations were employed investigate structural dynamic responses ions—Cd²⁺, Ni²⁺, Co³⁺, Pb²⁺, Pt²⁺. A series 200-ns MD metal-protein complexes was conducted at 300 K using GROMACS software CHARMM General Force Field. Key parameters analyzed included backbone root-mean-square deviation (RMSD), radius gyration (Rg), solvent-accessible surface area (SASA), fluctuations (RMSF). The results demonstrated that Cd²⁺, Pt²⁺ destabilized protein's structure, with notable effects observed critical regions EF loop, H-strand, AB loop. extent destabilization varied depending specific ion. findings emphasize need detailed residue-level analyses fully elucidate changes induced by their implications properties. This work provides valuable insights into behavior under lays groundwork developing β-lg-based nanosystems biomedical

Language: Английский