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A New Bio-active Surface For Protein Immobilisation Via Copper-free 'click' Between Azido Sam And Alkynyl Fischer Carbene Complex

机译:一种新的生物活性表面,可通过叠氮山姆和炔基菲舍尔卡宾复合物之间的无铜“点击”来固定蛋白质

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摘要

Fischer carbene complex anchored on glass or silicon surface using a Cu-free 'click' reaction allows facile and swift covalent grafting of protein molecules like Bovine Serum Albumin (BSA).rnProtein immobilisation on a surface using covalent linkage is vital to proteome research that includes development of microarray- and biochip-based sensors for high-throughput screening of protein structure and function, study of interaction between protein and other biomolecules, multianalyte immunoassay or enzyme assay for clinical diagnostics, etc. The linkage between the biomolecule and the inorganic solid support remains a critical variable for optimal performance of a sensor device. A wide range of protein immobilisation techniques have been developed and they are continuously being improved. It is well-recognised that a covalent bond between a biomolecule and a functionalised surface lasts longer and provides greater reproducibility than immobilisation obtained by non-covalent links. The covalent bond formation between the anchored protein and the glass surface must be extremely facile and should proceed under ambient conditions to conserve protein/enzyme structure and activity.
机译:利用无铜的“点击”反应将Fischer卡宾络合物固定在玻璃或硅表面上,可以轻松,快速地将诸如牛血清白蛋白(BSA)的蛋白质分子共价接枝。使用共价键将蛋白质固定在表面上对于蛋白质组学研究至关重要,其中包括基于微阵列和生物芯片的传感器的开发,用于高通量筛选蛋白质的结构和功能,研究蛋白质与其他生物分子之间的相互作用,用于临床诊断的多分析物免疫测定或酶测定等。生物分子与无机固体支持物之间的联系仍然是传感器设备最佳性能的关键变量。已经开发了各种各样的蛋白质固定技术,并且它们正在不断地改进。众所周知,与通过非共价键获得的固定化相比,生物分子和功能化表面之间的共价键持续时间更长,并且具有更高的可重复性。锚定蛋白质和玻璃表面之间的共价键形成必须非常容易,并且应在环境条件下进行以保留蛋白质/酶的结构和活性。

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