Probing recognition process between an antibody and an antigen using atomic force microscopy

被引：42

作者：

Chowdhury, PB ^{[1
]}

Luckham, PF ^{[1
]}

机构：

[1] Univ London Imperial Coll Sci Technol & Med, Dept Chem Engn, London SW7 2BY, England

来源：

COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS | 1998年 / 143卷 / 01期

关键词：

antigen; atomic force microscopy; antibody; probing; HSA;

D O I：

10.1016/S0927-7757(98)00408-7

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Specific recognition interaction between human serum albumin (HSA) antigen and its associated antibody has been investigated by probing with atomic force microscopy. The interacting tip and surface was chemically modified to covalently bond the proteins to both an AFM tip and a flat surface. This ensured that the proteins bound to the tip surface did not unbind upon interaction. Chemical modification was achieved by initially silanising the glass surface with aminopropyltrimethoxysilane to activate the surface to support immobilisation and then the addition of gluteraldehyde which acts as the bridging agent between the solid support and the protein to be immobilised. The force-distance profiles were taken in aqueous solutions. The force-distance profiles between the antigen antibody show a strong attractive interaction, with a binding force of similar to - 2000 pN. (C) 1998 Elsevier Science B.V.

引用

页码：53 / 57

页数：5

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