SFG analysis of surface bound proteins: a route towards structure determination.
SFG analysis of surface bound proteins: a route towards structure determination.
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DOI：
10.1039/c3cp50880c
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发表时间：
2013-08-14
期刊：
影响因子：
--
通讯作者：
Castner DG
中科院分区：
文献类型：
--
作者：
Weidner T;Castner DG
一旦将材料放置在生物环境中，该材料的表面就会迅速被蛋白质覆盖。这些结合蛋白的结构和功能在物质与生物环境的相互作用和交流中起着关键作用。因此，在分子水平上了解表面结合蛋白的结构是至关重要的。虽然X射线衍射法和溶液相核磁共振方法已经很好地确定了蛋白质在晶相或溶液相中的结构，但还没有一种相应的单一技术可以提供关于蛋白质表面或界面的相同水平的结构细节。然而，和频产生(SFG)振动光谱的最新进展显著提高了我们获得表面结合蛋白质和多肽的结构信息的能力。SFG与(1)选择性引入突变和同位素标记的蛋白质工程方法，(2)其他实验方法，如飞行时间二次离子质谱仪(ToF-SIMS)和近边X射线吸收精细结构(NEXAFS)等提供互补信息的其他实验方法，以及(3)扩展分子水平实验结果的分子动力学(MD)模拟相结合的多技术途径，是表征表面结合蛋白质和多肽结构的一条特别有前途的途径。通过使用具有明确结构的模型多肽和小蛋白，已经开发出确定主链和侧链到表面的方向的方法。
The surface of a material is rapidly covered with proteins once that material is placed in a biological environment. The structure and function of these bound proteins play a key role in the interactions and communications of the material with the biological environment. Thus, it is crucial to gain a molecular level understanding of surface bound protein structure. While X-ray diffraction and solution phase NMR methods are well established for determining the structure of proteins in the crystalline or solution phase, there is not a corresponding single technique that can provide the same level of structural detail about proteins at surfaces or interfaces. However, recent advances in sum frequency generation (SFG) vibrational spectroscopy have significantly increased our ability to obtain structural information about surface bound proteins and peptides. A multi-technique approach of combining SFG with (1) protein engineering methods to selectively introduce mutations and isotopic labels, (2) other experimental methods such as time-of-flight secondary ion mass spectrometry (ToF-SIMS) and near edge x-ray absorption fine structure (NEXAFS) to provide complementary information, and (3) molecular dynamic (MD) simulations to extend the molecular level experimental results is a particularly promising route for structural characterization of surface bound proteins and peptides. By using model peptides and small proteins with well-defined structures, methods have been developed to determine the orientation of both backbone and side chains to the surface.
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影响因子：
15
作者：
Chen, Xiaoyun;Boughton, Andrew P.;Chen, Zhan
通讯作者：
Chen, Zhan
影响因子：
3.9
作者：
Deighan, Michael;Pfaendtner, Jim
通讯作者：
Pfaendtner, Jim
影响因子：
15
作者：
Chen, XY;Tang, HZ;Chen, Z
通讯作者：
Chen, Z
影响因子：
15
作者：
Breen, Nicholas F.;Weidner, Tobias;Drobny, Gary P.
通讯作者：
Drobny, Gary P.
DOI：
10.1073/pnas.1108236108
发表时间：
2011-09-13
影响因子：
11.1
作者：
Boughton, Andrew P.;Yang, Pei;Chen, Zhan
通讯作者：
Chen, Zhan