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Characterization of a new maleimido functionalization of gold for surface plasmon resonance spectroscopy

: Hovestädt, M.; Memczak, H.; Pleiner, D.; Zhang, X.; Rappich, J.; Bier, F.F.; Stocklein, W.F.M.


Journal of Molecular Recognition : JMR 27 (2014), No.12, pp.707-713
ISSN: 0952-3499
ISSN: 1099-1352
Bundesministerium für Bildung und Forschung BMBF
03 IS2201 A
Journal Article
Fraunhofer IBMT ()

Para-maleimidophenyl (p-MP) modified gold surfaces have been prepared by one-step 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) and a protein with their specific antibodies were used as model systems. The peptides were modified with an N-terminal cysteine for covalent and directed coupling to the maleimido functionalized surface by means of Michael addition. The coupling yield of the peptide, the binding characteristics of antibody and the unspecific adsorption of the analytes were investigated. The results expand the spectrum of biosensors usable with p-MP by widely used SPR and support its potential to be versatile for several electrochemical and optical biosensors. This allows the combination of an electrochemical and optical read-out for a broad variety of biomolecular interactions on the same chip.