Specific antigen/antibody interactions measured by force microscopy

被引：374

作者：

Dammer, U

Hegner, M

Anselmetti, D

Wagner, P

Dreier, M

Huber, W

Guntherodt, HJ

机构：

[1] UNIV BASEL,INST PHYS,CH-4056 BASEL,SWITZERLAND

[2] CIBA GEIGY AG,RES SERV,CH-4002 BASEL,SWITZERLAND

[3] ETH ZURICH,DEPT BIOCHEM 2,CH-8092 ZURICH,SWITZERLAND

[4] F HOFFMANN LA ROCHE & CO LTD,CH-4002 BASEL,SWITZERLAND

来源：

BIOPHYSICAL JOURNAL | 1996年 / 70卷 / 05期

关键词：

D O I：

10.1016/S0006-3495(96)79814-4

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

Molecular recognition between biotinylated bovine serum albumin and polyclonal, biotin-directed IgG antibodies has been measured directly under various buffer conditions using an atomic force microscope (AFM). It was found that even highly structured molecules such as IgG antibodies preserve their specific affinity to their antigens when probed with an AFM in the force mode. We could measure the rupture force between individual antibody-antigen complexes. The potential and limitations of this new approach for the measurement of individual antigen/antibody interactions and some possible applications are discussed.

引用

页码：2437 / 2441

页数：5

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