蛋白质-表面活性剂组装结构的分子模拟

采用Langevin分子动力学方法模拟β模型蛋白与表面活性剂在溶液中形成的各种组装结构，考察了表面活性剂疏水性强度与浓度对蛋白质分子构象的影响.结果显示：弱疏水性表面活性剂可以在蛋白质表面自组装形成限制性空间，使被包覆的蛋白质的立体结构更为稳定;强疏水性的表面活性剂则可以与蛋白质疏水核心区的疏水基团形成复合物，而使蛋白质的立体结构被破坏，即蛋白质发生去折叠.上述模拟可再现相关实验结果，其展现的蛋白质结构转换微观图景对于表面活性剂的分子设计及其应用于生物加工过程具有指导作用.

Molecular simulation of protein-surfactant assembly in aqueous solution

Langevin dynamics was applied to investigate the molecular assembly formed between an all β-sheet model protein and surfactants with different hydrophobicity and concentration.It was shown that surfactants with weak hydrophobicity (ε_s≤0.20) formed a cage and thus enhanced the stability of the entrapped protein.While surfactants with strong hydrophobicity （ε_s>0.20）formed a complex with the hydrophobic beads located in the interior region of the protein and led to the structural decomposition of the protein，i.e.，protein unfolding.The above coarse-grained simulation agreed well with experimental observations reported elsewhere.The molecular insight into the protein conformational transition，as established by the present simulation，can be used to guide the design and application of surfactant in bio-processing engineering.