A Mussel Adhesive Protein Fused with the BC Domain of Protein A is a Functional Linker Material that Efficiently Immobilizes Antibodies onto Diverse Surfaces
- A Mussel Adhesive Protein Fused with the BC Domain of Protein A is a Functional Linker Material that Efficiently Immobilizes Antibodies onto Diverse Surfaces
- 서정현; 김창섭; 최유성[최유성]; 고우리[고우리]; 이지은[이지은]; 차형준[차형준]
- ESCHERICHIA-COLI; ORIENTED IMMOBILIZATION; STAPHYLOCOCCUS-AUREUS; MYTILUS-EDULIS; GOLD SURFACE; FC-BINDING; ARRAYS; FABRICATION; MICROARRAYS; EXPRESSION
- Issue Date
- WILEY-V C H VERLAG GMBH
- ADVANCED FUNCTIONAL MATERIALS, v.21, no.21, pp.4101 - 4108
- 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.
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