Single-molecule measurements and dynamical simulations of protein molecules near silicon substrates
Single-molecule measurements and dynamical simulations of protein molecules near silicon substrates
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DOI：
10.1088/0022-3727/41/9/095301
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发表时间：
2008-05-07
影响因子：
3.4
通讯作者：
Kawano, Satoyuki
中科院分区：
文献类型：
--
作者：
Hanasaki, Itsuo;Takahashi, Hiroto;Kawano, Satoyuki
蛋白质分子和无机基质之间的相互作用进行了实验和数值研究，以获得工程应用的生物大分子组装的基本见解。我们实验跟踪个人荧光标记的溶菌酶（F-溶菌酶）分子，扩散在蛋白质溶液和氧化硅（1 0 0）和玻璃板之间的界面附近。结果表明，F-溶菌酶分子在两种基质上的扩散系数比在本体溶液中的扩散系数小三个数量级以上。分子动力学模拟表明，溶菌酶在纯Si（1 1 1）和氧化Si（1 0 0）表面上的扩散系数由于分子吸附行为而大大降低，与实验结果吻合较好.此外，完整的原子描述的行为提供了详细的信息变形由于吸附过程。纯Si（111）上的溶菌酶发生了很大的变形，而氧化Si（100）上的溶菌酶没有发生变形，这表明基底表面条件对保持吸附的生物分子的结构即功能的重要性。
Interactions between protein molecules and inorganic substrates were studied both experimentally and numerically to obtain fundamental insight into the assembly of biomacromolecules for engineering applications. We experimentally traced individual fluorescent-labelled lysozyme (F-lysozyme) molecules, diffusing in the vicinity of interfaces between a protein solution and oxidized Si( 1 0 0) and glass plates. The results indicate that diffusion coefficients of F-lysozyme molecules on both substrates are more than three orders of magnitude smaller than those in a bulk solution. The molecular dynamics simulations reveal a drastically diminished diffusion coefficient of lysozyme on the substrates of pure Si( 1 1 1) and oxidized Si( 1 0 0) with a hydroxy-terminated surface compared with that in bulk solution due to molecular adsorption behaviour on the substrate, which is in good agreement with experimental results. Furthermore, full atomistic description of the behaviour provides detailed information of deformation due to the adsorption process. Lysozyme on pure Si( 1 1 1) undergoes substantial deformation whereas that on oxidized Si( 1 0 0) does not, which indicates the importance of substrate surface condition to preserve the structure, i.e. functionality of adsorbed biomolecules.