A nanoengineering approach for investigation and regulation of protein immobilization.
A nanoengineering approach for investigation and regulation of protein immobilization.
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DOI：
10.1021/nn800508f
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发表时间：
2008-11-25
期刊：
影响因子：
17.1
通讯作者：
Liu GY
中科院分区：
文献类型：
--
作者：
Tan YH;Liu M;Nolting B;Go JG;Gervay-Hague J;Liu GY
已知蛋白质与表面的附着敏感地取决于纳米尺度下结合位点的局部结构和环境。使用纳米接枝和反向纳米接枝，这两个原子力显微镜（AFM）为基础的光刻技术，蛋白质结合位点与明确的局部环境的设计和工程与纳米精度。三种蛋白质，山羊抗生物素免疫球蛋白G（IgG），溶菌酶和兔免疫球蛋白G，固定在这些工程化的表面。在抗体识别、通过伯胺残基的共价连接和表面结合的亲合基团中揭示了对蛋白质结合位点的尺寸和空间分布的强烈依赖。这项研究表明，基于AFM的纳米光刻技术能够生产蛋白质纳米结构，更重要的是，蛋白质表面相互作用在分子水平上可以通过改变结合域和它们的局部环境在纳米尺度上进行调节。
It is known that protein attachment to surfaces depends sensitively upon the local structure and environment of the binding sites at the nanometer scale. Using nanografting and reversal nanografting, both atomic force microscopy (AFM) - based lithography techniques, protein binding sites with well-defined local environments are designed and engineered with nanometer precision. Three proteins, goat-anti-biotin Immunoglobulin G (IgG), lysozyme and rabbit-Immunoglobulin G, are immobilized onto these engineered surfaces. Strong dependence on the dimension and spatial distribution of protein binding sites are revealed in antibody recognition, covalent attachment via primary amine residues and surface bound aldehyde-groups. This investigation indicates that AFM based nanolithography enables the production of protein nanostructures and more importantly, protein-surface interactions at a molecular level can be regulated by changing the binding domains and their local environment at nanometer scale.