蛋白质界面吸附的分子模拟
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- 英文论文题名：Molecular Simulations of Protein Adsorption
- 论文作者：周健
- 英文论文作者：Jian Zhou ; School of Chemistry and Chemical Engineering ; South China University of Technology
- 年：2016
- 作者机构：华南理工大学化学化工学院;
- 论文关键词：蛋白质吸附 ; 分子模拟
- 英文论文关键词：protein adsorption ; molecular simulation
- 会议召开时间：2016-07-01
- 会议录名称：中国化学会第30届学术年会摘要集-第三十一分会：胶体与界面化学
- 语种：中文
- 分类号：O629.73;O647.3
- 学会代码：ZGHY
- 会议名称：中国化学会第30届学术年会-第三十一分会 ; 胶体与界面化学
- 会议地点：中国辽宁大连
- 主办单位：中国化学会
- 学会名称：中国化学会
- 页数：1
- 文件大小：263k
- 原文格式：D
- 会议级别：全国
摘要
蛋白质吸附不仅广泛出现在很多基本的生物过程中,而且在蛋白质层析分离、固体基材的药物传递、生物传感器、生物燃料电池和医用生物材料等应用上也起到重要作用。对于这些过程和应用来说,一个关键的问题就是关于蛋白质在表面吸附的取向问题。控制抗体在表面的定向吸附,对于确保其活性位点远离表面,进而保证免疫分析中抗体的活性位朝向本体溶液是很有必要的。对于生物燃料电池的应用,为了确保快速电子转移,被吸附的细胞色素C中的血红素环取向应接近且垂直于表面。另一个决定吸附蛋白质活性的关键问题是蛋白质的吸附构象,即吸附蛋白质的构象要接近于它们的天然构象。本报告中,通过不同尺度的模型,包括胶体粒子、粗粒化和全原子模型,研究了带电表面的蛋白质取向和构型问题。我们使用了平行退火和副本交换分子动力学模拟方法。考察了表面电荷密度、符号以及溶液离子强度的影响。模拟结果显示,范德华作用和静电相互作用共同决定吸附蛋白的取向。吸附蛋白的电偶极与疏水偶极在决定蛋白在带电表面和疏水表面的取向起着重要作用。
Protein adsorption plays an important role in many applications such as protein chromatography,drug delivery on solid substrates,biosensors,biofuel cells and biomaterials.For these processes and applications,one key issue is the orientation of adsorbed proteins on surfaces.Controlled antibody adsorption orientation on surfaces is necessary to ensure that their active sites are away from the surface and accessible to bulk solution for immunoassay applications.For biofuel cell applications,to enable fast electron transfer,adsorbed cytochrome c should have an orientation with the heme ring close and perpendicular to surfaces.Another key issue that determines the activity of adsorbed proteins is their conformation(i.e.,how the conformation of the adsorbed protein resembles that of its native state).In this work,the protein orientation and conformation on charged surfaces are investigated by a hierarchical approach,i.e.,studied by colloidal,coarse-grained and all-atom models.Parallel tempering Monte Carlo and molecular dynamics simulations are used.Effects of surface charge density and sign,and solution ionic strength are examined in our simulations.Simulation results show that van der Waals and electrostatic interactions codetermine the orientation of adsorbed proteins.It is found that the electric dipole and hydrophobic dipole of adsorbed proteins play important roles in determining the protein orientation on charged and hydrophobic surfaces.
Protein adsorption plays an important role in many applications such as protein chromatography,drug delivery on solid substrates,biosensors,biofuel cells and biomaterials.For these processes and applications,one key issue is the orientation of adsorbed proteins on surfaces.Controlled antibody adsorption orientation on surfaces is necessary to ensure that their active sites are away from the surface and accessible to bulk solution for immunoassay applications.For biofuel cell applications,to enable fast electron transfer,adsorbed cytochrome c should have an orientation with the heme ring close and perpendicular to surfaces.Another key issue that determines the activity of adsorbed proteins is their conformation(i.e.,how the conformation of the adsorbed protein resembles that of its native state).In this work,the protein orientation and conformation on charged surfaces are investigated by a hierarchical approach,i.e.,studied by colloidal,coarse-grained and all-atom models.Parallel tempering Monte Carlo and molecular dynamics simulations are used.Effects of surface charge density and sign,and solution ionic strength are examined in our simulations.Simulation results show that van der Waals and electrostatic interactions codetermine the orientation of adsorbed proteins.It is found that the electric dipole and hydrophobic dipole of adsorbed proteins play important roles in determining the protein orientation on charged and hydrophobic surfaces.
引文
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