Citation: ZHOU Wen-Wen, LIAN Jie, HU Ke-Jia, GAO Yun-Hua, XU Bai. Effect of Surface Chemical Properties of a Silicon Chip on Antibody Immobilization[J]. Acta Physico-Chimica Sinica, ;2010, 26(10): 2821-2827. doi: 10.3866/PKU.WHXB20101016 shu

Effect of Surface Chemical Properties of a Silicon Chip on Antibody Immobilization

ZHOU Wen-Wen ^1,2 ,
LIAN Jie ^1,2 ,
HU Ke-Jia ^1,2 ,
GAO Yun-Hua ^1, ,
XU Bai ^1,

1.
1. Key Laboratory of Photochemical Conversion and Optoelectronic Materials, Technical Institute of Physics and Chemistry,Chinese Academy of Sciences, Beijing 100190, P. R. China;
2. Graduate University of Chinese Academy of Sciences,Beijing 100049, P. R. China

Received Date: 22 April 2010
Available Online: 27 September 2010
Fund Project: 国家自然科学基金(20975106) (20975106) 中国科学院知识创新工程重要方向项目(KJCX2-YW-M15) 及国家重大专项(2008ZX08012-001) 资助 (KJCX2-YW-M15) 及国家重大专项(2008ZX08012-001)

The key to constructing a protein microarray is the stable immobilization of proteins and the retention of their biological activities. In this study, immobilization of the carcinoembryonic antigen (CEA) antibody onto a silicon dioxide surface was investigated by physical adsorption, direct chemical covalent conjugation, spacer-added chemical covalent conjugation, and biological affinity interactions. Based on the specific antibody-antigen interactions, the sandwich reaction, enzyme-linked immunosorbent assay (ELISA) was chosen to evaluate various immobilization strategies. The most efficient immobilization strategy was with glutaraldehyde as a coupling reagent between the CEA antibody and the amino surface. The attachment of a spacer-armcomprising poly-L-lysine significantly improved the immobilization efficiency and simultaneously decreased nonspecific adsorption. High immobilization efficiency and stronger nonspecific adsorption were also observed when the CEA antibody was immobilized by bioaffinity interactions.
- Protein microarray,
- Antibody immobilization,
- Sandwich reaction,
- Enzyme-linked immunosorbent assay,
- Amino surface,
- Glutaraldehyde,
- Poly-L-lysine
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