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石墨上蛋白质变性状态的单分子水平原子力显微镜可视化。

AFM visualization at a single-molecule level of denaturated states of proteins on graphite.

作者信息

Barinov Nikolay A, Prokhorov Valery V, Dubrovin Evgeniy V, Klinov Dmitry V

机构信息

Federal Research and Clinical Center of Physical-Chemical Medicine, Malaya Pirogovskaya, 1a, Moscow 119435 Russian Federation.

Federal Research and Clinical Center of Physical-Chemical Medicine, Malaya Pirogovskaya, 1a, Moscow 119435 Russian Federation; Lomonosov Moscow State University, Leninskie gory, 1-2, Moscow 119991, Russian Federation.

出版信息

Colloids Surf B Biointerfaces. 2016 Oct 1;146:777-84. doi: 10.1016/j.colsurfb.2016.07.014. Epub 2016 Jul 6.

DOI:10.1016/j.colsurfb.2016.07.014
PMID:27451365
Abstract

Different graphitic materials are either already used or believed to be advantageous in biomedical and biotechnological applications, e.g., as biomaterials or substrates for sensors. Most of these applications or associated important issues, such as biocompatibility, address the problem of adsorption of protein molecules and, in particular the conformational state of the adsorbed protein molecule on graphite. High-resolution AFM demonstrates highly oriented pyrolytic graphite (HOPG) induced denaturation of four proteins of blood plasma, such as ferritin, fibrinogen, human serum albumin (HSA) and immunoglobulin G (IgG), at a single molecule level. Protein denaturation is accompanied by the decrease of the heights of protein globules and spreading of the denatured protein fraction on the surface. In contrast, the modification of HOPG with the amphiphilic oligoglycine-hydrocarbon derivative monolayer preserves the native-like conformation and provides even more mild conditions for the protein adsorption than typically used mica. Protein unfolding on HOPG may have universal character for "soft" globular proteins.

摘要

不同的石墨材料已经被应用或被认为在生物医学和生物技术应用中具有优势,例如作为生物材料或传感器的基底。这些应用中的大多数或相关的重要问题,如生物相容性,都涉及蛋白质分子的吸附问题,特别是吸附在石墨上的蛋白质分子的构象状态。高分辨率原子力显微镜在单分子水平上证明了高度定向热解石墨(HOPG)可诱导血浆中的四种蛋白质变性,如铁蛋白、纤维蛋白原、人血清白蛋白(HSA)和免疫球蛋白G(IgG)。蛋白质变性伴随着蛋白质球状体高度的降低以及变性蛋白质部分在表面的扩散。相比之下,用两亲性低聚甘氨酸-烃衍生物单层修饰HOPG可保留天然样构象,并且比通常使用的云母为蛋白质吸附提供更温和的条件。HOPG上的蛋白质展开可能对“软”球状蛋白质具有普遍特征。

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