The dendron-modified surface can be also applied to enhance ligand-protein interaction. Streptavidin(SA)-biotin interaction was investigated by SPR (Surface Plasmon Resonance) spectroscopy. For a comparison, we selected a representative set of mixed SAMs composed of 16-mercaptohexadecanoic acid (16-MHA) and 11-mercaptoundecanol (11-MUOH), and investigated the same interaction. Table1 shows that the NSB surface is efficient in achieving specific and efficient Streptavidin-biotin interaction. When compared with the mixed SAMs, the comparable binding level of SA was observed with the biotinylated NSB surface even at a lower biotin density. The result demonstrates that appropriate spacing control is very important in enhancing biomolecular interaction on surface.

Table 1. The increase in response unit (ΔRU) upon binding of SA to various biotin immobilized layers.