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Title 

Controlled antibody immobilization onto immunoanalytical platforms by synthetic peptide

Authors 

Yongwon JungH J KangJeong Min LeeS O JungW S YunSang Jeon ChungBong Hyun Chung

Publisher 

Elsevier

Issue Date 

2008

Citation 

Analytical Biochemistry, vol. 374, no. 1, pp. 99-105

Keywords 

antibody immobilizationbiochipbiosensorFc-binding peptideimmunoassayantibodysynthetic peptideprotein immobilizationantibodies

Abstract 

Antibody immobilization on a solid surface is inevitable in the preparation of immunochips/sensors. Antibody-binding proteins such as proteins A and G have been extensively employed to capture antibodies on sensor surfaces with right orientations, maintaining their full functionality. Because of their synthetic versatility and stability, in general, small molecules have more advantages than proteins. Nevertheless, no small molecule has been used for oriented and specific antibody immobilization. Here is described a novel strategy to immobilize an antibody on various sensor surfaces by using a small antibody-binding peptide. The peptide binds specifically to the Fc domain of immunoglobulin G (IgG) and, therefore, affords a properly oriented antibody surface. Surface plasmon resonance analysis indicated that a peptide linked to a gold chip surface through a hydrophilic linker efficiently captured human and rabbit IgGs. Moreover, antibodies captured by the peptide exhibited higher antigen binding capacity compared with randomly immobilized antibodies. Peptide-mediated antibody immobilization was successfully applied on the surfaces of biosensor substrates such as magnetic particles and glass slides. The antibody-binding peptide conjugate introduced in this work is the first small molecule linker that offers a highly stable and specific surface platform for antibody immobilization in immunoassays.

ISSN 

0003-2697

Link 

http://dx.doi.org/10.1016/j.ab.2007.10.022

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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