@article{HovestaedtMemczakPleineretal.2014,
  author    = {Hovestaedt, Marc and Memczak, Henry and Pleiner, Dennis and Zhang, Xin and Rappich, Joerg and Bier, Frank Fabian and St{\"o}cklein, Walter F. M.},
  title     = {Characterization of a new maleimido functionalization of gold for surface plasmon resonance spectroscopy},
  series = {Journal of molecular recognition : an international journal devoted to research on specific molecular recognition in chemistry, biology, biotechnology and medicine},
  volume    = {27},
  journal   = {Journal of molecular recognition : an international journal devoted to research on specific molecular recognition in chemistry, biology, biotechnology and medicine},
  number    = {12},
  publisher = {Wiley-Blackwell},
  address   = {Hoboken},
  issn      = {0952-3499},
  doi       = {10.1002/jmr.2396},
  pages     = {707 -- 713},
  year      = {2014},
  abstract  = {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. Copyright (c) 2014 John Wiley \& Sons, Ltd.},
  language  = {en}
}