Precipitantless Crystallization of Protein Molecules Induced by High Surface Potential

Precipitantless Crystallization of Protein Molecules Induced by High Surface Potential
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高表面电势诱导的蛋白质分子无沉淀结晶

DOI:
10.1021/acs.cgd.6b00833
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发表时间:
2016
影响因子:
3.8
通讯作者:
A. Ghatak
A. Ghatak
中科院分区:
化学2区
文献类型:
--
作者:
A. Ghatak;A. Ghatak

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在蛋白质结晶的背景下,具有异质形貌特征的表面装饰降低了成核的能垒,从而促进结晶;然而,需要使用沉淀剂。在这里,我们通过利用纳米级表面起伏和基材上电荷的综合作用,消除了对此类沉淀剂的需求。使用表面不稳定性作为在聚合物材料上生成此类特征的工具,我们表明纳米特征(<10 nm)的固有曲率与表面电荷相结合导致电势空间梯度高达 140 V·μm–1,其中曲率达到最大。这些表面显示出任何其他传统工艺无法实现的显着诱导成核的能力。它们诱导蛋白质的无沉淀成核,从两种或多种物质的混合物中定向结晶特定蛋白质,甚至从蛋白质混合物中同时结晶。这些结果意味着大规模分子有序化......
In the context of protein crystallization, surface decorated with heterogeneous topographical features decreases the energy barrier for nucleation, thereby facilitating crystallization; a precipitant is, nevertheless, required to be used. Here we eliminate the need of such precipitant by using a combined effect of nanoscopic surface undulations and charges on a substrate. Using surface instabilities as a tool for generating such features on polymeric materials, we show that intrinsic curvature of nanofeatures (<10 nm) coupled with surface charges lead to spatial gradient in potential as high as 140 V·μm–1, where curvature gets maximum. These surfaces show remarkable ability to induce nucleation not achieved by any other conventional process. They induce precipitantless nucleation of proteins, directed crystallization of a specific protein from a mixture of two or more species, and even simultaneous crystallization from a mixture of proteins. These results signify large scale molecular ordering at the bulk...
DOI: 10.1038/nmeth.f.203
发表时间: 2008-02-01
期刊: NATURE METHODS
影响因子: 48
作者:
Chayen, Naomi E.;Saridakis, Emmanuel
通讯作者: Saridakis, Emmanuel