Adsorption Orientation and Binding Motifs of Lysozyme and Chymotrypsin on Amorphous Silica
Adsorption Orientation and Binding Motifs of Lysozyme and Chymotrypsin on Amorphous Silica
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DOI：
10.1021/acs.jpcc.5b00560
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发表时间：
2015-03
影响因子：
3.7
通讯作者：
Nils Hildebrand;S. Köppen;Ludmilla Derr;Kaibo Li;M. Koleini;K. Rezwan;L. Ciacchi
中科院分区：
文献类型：
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作者：
Nils Hildebrand;S. Köppen;Ludmilla Derr;Kaibo Li;M. Koleini;K. Rezwan;L. Ciacchi
采用分子动力学方法研究了α-凝乳胰蛋白酶和蛋清溶菌酶在无定形二氧化硅上的吸附，并与吸附实验进行了比较。在DLVO理论的水平上计算了隐式溶剂中蛋白质表面相互作用的分布。这揭示了胰凝乳酶的优先吸附取向，这是由它的大偶极矩驱动的，它的α-螺旋区指向表面。相反，溶菌酶吸附的取向偏好不太明确，它以侧面方向接近表面，证实了先前的结果。然后进行了显式溶剂MD模拟，以分析蛋白质表面接触的形成和稳定性。虽然在研究的短模拟时间内（高达300 ns）没有发生明显的构象变化，但模拟清楚地揭示了吸附基的存在，包括正电荷、负电荷、极性甚至非极性残基。稳定吸附源…
The adsorption of α-chymotrypsin and hen egg white lysozyme on amorphous silica is studied by molecular dynamics (MD) simulations in comparison with adsorption experiments. Protein–surface interaction profiles are computed in implicit solvent at the level of DLVO theory. These reveal a preferential adsorption orientation for chymotrypsin, driven by its large dipole moment, with its α-helical regions pointing toward the surface. Instead, a less clear orientational preference characterizes lysozyme adsorption, which approaches the surface in a side-on orientation, confirming previous results. Explicit-solvent MD simulations are then performed to analyze the formation and stability of protein–surface contacts. While no significant conformational changes take place in the short simulation time investigated (up to 300 ns), the simulations clearly reveal the presence of adsorption motifs comprising both positively charged, but also negatively charged, polar and even nonpolar residues. Stable adsorption originat...