Assembling of engineered IgG-binding protein on gold surface for highly oriented antibody immobilization

被引：112

作者：

Kanno, S ^{[1
]}

Yanagida, Y ^{[1
]}

Haruyama, T ^{[1
]}

Kobatake, E ^{[1
]}

Aizawa, M ^{[1
]}

机构：

[1] Tokyo Inst Technol, Grad Sch Biosci & Biotechnol, Dept Biol Informat, Midori Ku, Yokohama, Kanagawa 2268501, Japan

来源：

JOURNAL OF BIOTECHNOLOGY | 2000年 / 76卷 / 2-3期

关键词：

B-domain; IgG-binding protein; immobilization of antibody; protein A; self-assemble;

D O I：

10.1016/S0168-1656(99)00186-8

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

The B-domain, which is one of IgG-binding domains of staphylococcal protein A, was repeated five times and a cysteine residue was introduced at its C-terminus by a genetic engineering technique. The resulting protein, designated B5C1, retained the same IgG-binding activity as native protein A. The B5C1 was assembled on a gold plate surface by utilizing a strong affinity between thiol of cysteine and a gold surface. IgG-binding activity of B5C1 on a gold surface was much higher than that of physically adsorbed B5, which lacks cysteine residue. Furthermore, antigen-binding activity of immobilized antibody molecules through the use of assembled B5C1 on a gold surface was about 4.3 times higher than that of physically adsorbed antibody molecules. Immobilization of highly oriented antibody molecules was realized with the engineered IgG-binding protein. (C) 2000 Elsevier Science B.V. All rights reserved.

引用

页码：207 / 214

页数：8

共 19 条

[1] STUDY OF IMMUNOGLOBULIN-G THIN-LAYERS OBTAINED BY THE LANGMUIR-BLODGETT METHOD - APPLICATION TO IMMUNOSENSORS [J].