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Title 

Photoactivable antibody binding protein: site-selective and covalent coupling of antibody

Authors 

Yongwon JungJeong Min LeeJ W KimJ YoonHyunmin ChoBong Hyun Chung

Publisher 

American Chemical Society

Issue Date 

2009

Citation 

Analytical Chemistry, vol. 81, no. 3, pp. 936-942

Keywords 

antibodybacterial proteinIgG Fc binding protein, streptococcusIgG Fc-binding protein, streptococcusbinding siteantibodiesbacterial proteinsbinding sites

Abstract 

Here we report new photoactivable antibody binding proteins, which site-selectively capture antibodies and form covalent conjugates with captured antibodies upon irradiation. The proteins allow the site-selective tagging and/or immobilization of antibodies with a highly preferred orientation and omit the need for prior antibody modifications. The minimal Fc-binding domain of protein G, a widely used antibody binding protein, was genetically and chemically engineered to contain a site-specific photo cross-linker, benzophenone. In addition, the domain was further mutated to have an enhanced Fc-targeting ability. This small engineered protein was successfully cross-linked only to the Fc region of the antibody without any nonspecific reactivity. SPR analysis indicated that antibodies can be site-selectively biotinylated through the present photoactivable protein. Furthermore, the system enabled light-induced covalent immobilization of antibodies directly on various solid surfaces, such as those of glass slides, gold chips, and small particles. Antibody coupling via photoactivable antibody binding proteins overcomes several limitations of conventional approaches, such as random chemical reactions or reversible protein binding, and offers a versatile tool for the field of immunosensors.

ISSN 

0003-2700

Link 

http://dx.doi.org/10.1021/ac8014565

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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