Laboratoire PEC, UMR CNRS 6087, Université du Maine, A.O. Messiaen, 72085, Le Mans, France.
Anal Bioanal Chem. 2010 Oct;398(3):1249-55. doi: 10.1007/s00216-010-4032-x. Epub 2010 Aug 5.
We present a new and advanced methodology, developed for surface functionalisation of gold and to study immobilisation of an immuno-specific system of proteins. A combination of electrochemical quartz crystal microbalance and Raman spectroscopy techniques allowed a complete understanding of the system starting from surface functionalisation and progressing to the functional structure analysis of immobilised proteins. A simple electrochemical procedure was formulated to prepare sulphonyl chloride terminated gold surfaces that form a strong sulphonamide bond with the receptor protein staphylococcal protein A (SpA). On the SpA grafted surfaces, the immobilisation of a human IgG and consecutive binding of an immuno-specific anti-human IgG was observed. The surface functional groups form a strong interaction with SpA without disturbing its functional properties. The native functional structure of SpA and also the IgGs was found to be retained in their immobilised state.
我们提出了一种新的先进方法,用于金的表面功能化,并研究蛋白质免疫特异性系统的固定化。电化学石英晶体微天平和拉曼光谱技术的组合允许从表面功能化开始,全面了解该系统,并进一步分析固定化蛋白质的功能结构。制定了一种简单的电化学程序来制备磺酰氯封端的金表面,该表面与受体蛋白葡萄球菌蛋白 A(SpA)形成强磺酰胺键。在 SpA 接枝的表面上,观察到了人 IgG 的固定化和随后的免疫特异性抗人 IgG 的结合。表面功能基团与 SpA 形成强相互作用,而不会干扰其功能特性。发现 SpA 和 IgG 的天然功能结构在其固定化状态下得以保留。