Characterization of a new maleimido functionalization of gold for surface plasmon resonance spectroscopy. Issue 12 (9th October 2014)

• Record Type: Journal Article
• Authors: Hovestädt, Marc; Memczak, Henry; Pleiner, Dennis; Zhang, Xin; Rappich, Jörg; Bier, Frank F.; Stöcklein, Walter F. M.
• Is Part Of: Journal of molecular recognition. Volume 27:Issue 12(2014:Dec.)
• Page Start: 707
• Page End: 713
• Publication Date: 2014-10-09
• Subjects: Molecular recognition -- Periodicals; Models, Molecular -- Periodicals; Molecular Conformation -- Periodicals; Molecular Sequence Data -- Periodicals; Molecular Structure -- Periodicals; Carrier Proteins -- Periodicals; 572.8
• DOI: 10.1002/jmr.2396
• Languages: English
• ISSNs: 0952-3499

Abstract

<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Para‐maleimidophenyl (<italic>p</italic>‐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 <italic>p</italic>‐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. Copyright © 2014 John Wiley &amp; Sons, Ltd.</p> </abstract>