食品与机械2025，Vol.41Issue(2)：33-40,8.DOI:10.13652/j.spjx.1003.5788.2024.80574
食盐对β-乳球蛋白与花青素结合及其分子动力学的影响
Molecular dynamics study of salt on the binding of β-lactoglobulin to anthocyanins
摘要
Abstract
[Objective]To investigate the effects of different NaCl concentrations on the binding of proteins to small molecules.[Methods]The β-lactoglobulin and anthocyanin were selected as the target protein and small molecule,respectively.Molecular dynamics simulations were conducted to study the binding patterns and protein structural changes under five NaCl concentrations(0,0.25,0.50,0.75,and 1.00 mol/L).[Results]Anthocyanin mainly bound to the hydrophobic cavity of β-lactoglobulin.In the 150 ns molecular dynamics simulations,the protein structure remained stable at each NaCl concentration,and its binding with the small molecule was steady.However,with the increase in NaCl concentration,the hydrogen bonds between proteins,hydrophobic surface area,and α-helix content decreased,while the β-sheet content increased within the 0.75 mol/L NaCl concentration range.The binding free energy of the two components first increased with NaCl concentration,reached a maximum at 0.50 mol/L,and then gradually decreased.At 1.00 mol/L,it was even much lower than the control group,mainly due to the simultaneous weakening of van der Waals forces,hydrogen bonding,and hydrophobic interactions under 1.00 mol/L NaCl.Small molecules also moved from the interior of the hydrophobic cavity toward the surface at the protein binding site.[Conclusion]The amount of NaCl added in the food system significantly affects the binding of proteins to small plant molecules,which may further affect the properties of proteins and the biological activity of small molecules.关键词
NaCl/花青素/β-乳球蛋白/分子动力学Key words
NaCl/anthocyanins/β-lactoglobulin/molecular dynamics引用本文复制引用
管思彤,胡霄,黄业传..食盐对β-乳球蛋白与花青素结合及其分子动力学的影响[J].食品与机械,2025,41(2):33-40,8.基金项目
湖北省大学生创新创业训练计划项目(编号:S202411336027) （编号:S202411336027）
湖北省科技计划项目(编号:2022BEC031) （编号:2022BEC031）
