Hovestädt, M.; Memczak, H.; Pleiner, D.; Zhang, X.; Rappich, J.; Bier, F.; Stöcklein, W.: Characterization of a new maleimido functionalization of gold for surface plasmon resonance spectroscopy. Journal of Molecular Recognition 27 (2014), p. 707-713

Para-Maleimidophenyl (p-MP) modified gold surfaces have been prepared by electrochemical deposition and used in surface plasmon resonance (SPR) studies. Therefore, a FITC mimotope peptide (MP1, 12 aa), a human mucin 1 epitope peptide (MUC, 9 aa) as well as a protein with their specific antibodies were used as model systems. The peptides were modified with an N-terminal cysteine for covalent coupling to the maleimido functionalized surface by means of Michael addition. The coupling yield of the peptide, the binding characteristics of antibody, and unspecific adsorption of the analytes were investigated. The results indicated that the p-MP modified gold surface has the potential to be versatile not only for electrochemical, as shown previously, but also for optical biosensors and allows the combination of an electrochemical and optical readout for a broad variety of biomolecular interactions on the same chip.