A unique antibody-binding protein, (E12B2)n, was genetically synthesized, w
hich was characterized by a hydrophobic peptide, E12, at one terminus and a
n antibody-binding peptide, B2, at the other. It was clarified by atomic fo
rce microscopy (AFM) imaging that this protein was efficiently self-assembl
ed on a hydrophobic solid surface. (E12B2)n self-assembled on a microplate
exhibited an excellent performance of antibody-binding affinity. The propos
ed design of antibody-binding protein seems promising in immobilizing antib
ody molecules on hydrophobic solid surfaces.