SPR studies of the nonspecific adsorption kinetics of human IgG and BSA on gold surfaces modified by self-assembled monolayers (SAMs)
SPR studies of the nonspecific adsorption kinetics of human IgG and BSA on gold surfaces modified by self-assembled monolayers (SAMs)
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DOI：
10.1006/jcis.1996.4586
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发表时间：
1997-01-01
影响因子：
9.9
通讯作者：
Vanderah, DJ
中科院分区：
文献类型：
--
作者：
Silin, V;Weetall, H;Vanderah, DJ
在具有以下末端基团的自组装烷基硫醇单层 (SAM) 修饰的金表面上研究了人免疫球蛋白 G (hIgG) 和牛血清白蛋白 (BSA) 的非特异性结合：CH3、C6H4OH、COO-、NH2、OH 和寡聚环氧乙烷 (OEO)。利用表面等离振子共振 (SPR) 技术和 How 池，实时监测 hIgG 和 BSA 吸附和解吸的动力学。吸附在 SAM 上的 hIgG 分子的表面浓度按以下顺序降低：CH3 > C6H5OH > COO- > NH2 > OH > OEO SAM 表面。 BSA 与 SAM 表面的结合按顺序降低：C6H5OH > CH3 > COO- > NH2 > OH > OEO。结果表明，在 OEO SAM 上，这些蛋白质的表面浓度低于 0.5 ng/cm(2)（我们的 SPR 装置的检测限），比疏水性 CH3 封端的 SAM 表面上的浓度低约 10(3) 倍。蛋白质吸附的结合曲线动力学是根据吸附蛋白质的多种状态来描述的，这些状态涉及不同表面的多点疏水、静电和氢键相互作用以及由吸附蛋白质的解折叠引起的蛋白质横向相互作用。 (C) 1997 学术出版社
The nonspecific binding of human immunoglobulin G (hIgG) and bovine serum albumin (BSA) was studied on gold surfaces modified by self-assembled alkyl thiol monolayers (SAMs) with the following terminal groups: CH3, C6H4OH, COO-, NH2, OH, and oligoethylene oxide (OEO). The kinetics of hIgG and BSA adsorption and desorption were monitored in real time utilizing the surface plasmon resonance (SPR) technique with a how cell. The surface concentration of hIgG molecules adsorbed on the SAMs decreased in the order: CH3 > C6H5OH > COO- > NH2 > OH > OEO SAM surfaces. Binding of BSA to the SAM surfaces decreased in the order: C6H5OH > CH3 > COO- > NH2 > OH > OEO. The results show that on the OEO SAM, the surface concentration of these proteins was less than 0.5 ng/cm(2) (the detection limit of our SPR device) and approximately 10(3) times less than that on the hydrophobic CH3-terminated SAM surfaces. The kinetics of the binding curves for the adsorption of the proteins are described in terms of multiple states of adsorbed proteins that involve multipoint hydrophobic, electrostatic, and hydrogen bond interactions for the different surfaces and protein lateral interactions caused by the unfolding of adsorbed proteins. (C) 1997 Academic Press