Analysis for peptide binding to porphyrin using surface plasmon resonance

The development of a novel high-sensitivity biosensor to detect low molecular weight chemicals is required from the viewpoint of monitoring the environment. In this study, the potential of a peptide as a ligand instead of an antibody was investigated. The porphyrin (H2TMpyP) was used as a model target compound. The porphyrin sandwiching peptide (PSP) was used as a model ligand peptide and the surface plasmon resonance (SPR) method was used for analysis of binding affinity. Porphyrin binding could be detected and the binding constant of PSP immobilized on SPR chip to H2TMpyP was about 105 M−1.