A Mussel Adhesive Protein Fused with the BC Domain of Protein A is a Functional Linker Material that Efficiently Immobilizes Antibodies onto Diverse Surfaces
SCIE
SCOPUS
- Title
- A Mussel Adhesive Protein Fused with the BC Domain of Protein A is a Functional Linker Material that Efficiently Immobilizes Antibodies onto Diverse Surfaces
- Authors
- Chang Sup Kim; Yoo Seong Choi; Wooree Ko; Jeong Hyun Seo; Jieun Lee; Cha, HJ
- Date Issued
- 2011-11-08
- Publisher
- Wiley-VCH
- Abstract
- The efficient immobilization of antibodies onto solid surfaces is vital for the sensitivity and specificity of various immunoassays and immunosensors. A novel linker protein, BC-MAP, is designed and produced in Escherichia coli by genetically fusing mussel adhesive protein (MAP) with two domains (B and C) of protein A (antibody-binding protein) for efficient antibody immobilization on diverse surfaces. Through direct surface-coating analyses, it is found that BC-MAP successfully coats diverse surfaces including glass, polymers, and metals, but the BC domain alone does not. Importantly, antibodies are efficiently immobilized on BC-MAP-coated surfaces, and the immobilized antibodies interact selectively with their corresponding antigen. Quartz-crystal-microbalance analyses show that BC-MAP has excellent antibody-binding ability compared to that of BC protein on gold surfaces. These results demonstrate that the MAP domain, with uniquely strong underwater adhesive properties, plays a role in the direct and efficient coating of BC-MAP molecules onto diverse surfaces that lack additional surface treatment, and the BC domain of BC-MAP contributes to the selective and oriented immobilization of antibodies on BC-MAP-coated surfaces. Thus, the BC-MAP fusion protein could be a valuable novel linker material for the facile and efficient immobilization of antibodies onto diverse solid supports.
- Keywords
- ESCHERICHIA-COLI; ORIENTED IMMOBILIZATION; STAPHYLOCOCCUS-AUREUS; MYTILUS-EDULIS; GOLD SURFACE; FC-BINDING; ARRAYS; FABRICATION; MICROARRAYS; EXPRESSION
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/16709
- DOI
- 10.1002/ADFM.201100710
- ISSN
- 1616-301X
- Article Type
- Article
- Citation
- ADVANCED FUNCTIONAL MATERIALS, vol. 21, no. 21, page. 4101 - 4108, 2011-11-08
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