Effect of Surfactants on Surface-Induced Denaturation of Proteins: Evidence of an Orientation-Dependent Mechanism
Effect of Surfactants on Surface-Induced Denaturation of Proteins: Evidence of an Orientation-Dependent Mechanism
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DOI：
10.1021/acs.jpcb.8b07368
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发表时间：
2018-12-13
影响因子：
3.3
通讯作者：
Shea, Joan-Emma
中科院分区：
文献类型：
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作者：
Arsiccio, Andrea;McCarty, James;Shea, Joan-Emma
当蛋白质与界面结合时，蛋白质结构的变化可能导致蛋白质功能的丧失。我们调查的机制，表面活性剂分子可以抵消表面诱导的蛋白质变性，通过详细研究的GB 1肽在空气-水，冰水，和二氧化硅-水界面的稳定性，使用分子动力学模拟加上metadaptics。我们的模拟结果表明，空气-水界面，并在较小程度上，冰-水界面破坏蛋白质和表面之间的直接相互作用，破坏蛋白质的疏水核心的蛋白质，而弱相互作用的二氧化硅表面稳定的蛋白质通过限制效应。添加表面活性剂Tween 80导致蛋白质在空气-水和冰-水表面的稳定化和在水-二氧化硅界面的温和去稳定化。我们表明，表面活性剂的两亲性是其稳定/不稳定的效果的关键，与取向依赖的机制，其中蛋白质是稳定的，当表面活性剂的亲水头指向蛋白质。
When proteins bind to interfaces, the resulting changes in protein structure can lead to loss of protein function. We investigate the mechanism by which surfactant molecules can counteract surface-induced protein denaturation through a detailed study of the stability of the GB1 peptide at the air-water, ice-water, and silica-water interfaces using molecular dynamics simulations coupled with metadynamics. Our simulations reveal that the air-water interface and, to a lesser extent, the ice-water interface destabilize the protein by direct interactions between the protein and surface that disrupt the hydrophobic core of the protein, while the weakly interacting silica surface stabilizes the protein through confinement effects. Addition of the surfactant Tween 80 leads to stabilization of the protein at the air-water and ice-water surfaces and mild destabilization at the water-silica interface. We show that the amphiphilic nature of the surfactant is key to its stabilizing/destabilizing effect, with an orientation-dependent mechanism in which the protein is stabilized when the hydrophilic heads of the surfactant point toward the protein.