earticle

영어

Oriented antibody immobilization is very important in the development of immunological analytic devices. To immobilize antibodies on assay surfaces, most of all technologies rely on physical adsorption or covalent coupling of the protein. However, these methods often cause reduced
antigen binding affinity due to random orientation, denaturation, and chemical modification of antibodies. To overcome this drawback, we suggested a novel strategy to immobilize an antibody on various sensor surfaces by fusion protein with Fc-binding peptide and mussel adhesive protein. Fc-binding peptide can afford oriented antibody immobilization on sensor surfaces by binding Fc region of immunoglobulin G. Mussel adhesive protein from Mytilus galloprovincialis can attach a variety of surfaces and therefore, the fusion protein can attach various sensor surfaces without loss of activity. Through SDS-PAGE analysis, we identified whether the fusion protein capture immunoglobulin G or not and the species specificity of the fusion protein. Quartz Crystal Microbalance (QCM) analysis indicated antibody immobilization
by the fusion protein exhibited higher antigen binding capability than random antibody immobilization.