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    Functionalisation of gold surfaces with thiolate SAMs: Topography/bioactivity relationship – A combined FT-RAIRS, AFM and QCM investigation

    Year: 2007

    Journal: Surface Science, Volume 601, Issue 18, 15 September 2007, Pages 3850-3855, 20111221

    Authors: E. Briand, C. Gu, S. Boujday, M. Salmain, J.M. Herry and C.M. Pradier

    Organizations: Laboratoire de Réactivité de Surface, UMR CNRS 7609, Université Pierre et Marie Curie, Tour 54–55, courrier 178, 4 place Jussieu, 75252 Paris Cedex 05, France, Laboratoire de Chimie et Biochimie des Complexes Moléculaires, UMR CNRS 7576, Ecole Nationale Supérieure de Chimie de Paris, 75231 Paris Cedex 05, France, Unité de Recherche en Bioadhésion et Hygiène des Matériaux, Institut National de la Recherche Agronomique 25, avenue de la République, F-91744 Massy Cedex, France

    Immobilisation of rabbit immunoglobulin G (rIgG) was performed by affinity binding to protein A (PrA) covalently bound to three different thiolate self-assembled monolayers (SAMs), (i) a mixed SAM of mercaptoundecanoic acid (MUA) and mercaptohexanol (C6OH) at a molar ratio of 1–3, (ii) a pure SAM of MUA and (iii) a pure SAM of cystamine (CA). A comparative study of anti-rIgG recognition process on these three surfaces was achieved in order to assess the influence of the attachment layer topography and composition upon the sensor quality. Functionalised gold-coated surfaces were characterised by three complementary analytical techniques, namely atomic force microscopy (AFM), polarization modulation–reflection-adsorption infrared spectroscopy (PM-RAIRS) and quartz crystal microbalance (QCM). PM-RAIRS and AFM revealed that the three SAMs were formed on the gold surfaces. AFM observations made it clear that the thiolate and PrA layers were rather homogeneous in the case of pure MUA and CA SAMs, as compared to the MUA/C6OH mixed SAM on which PrA aggregates were observed. Though the highest amount of antibody was bound to the PrA on CA layer, higher anti-rIgG over IgG ratios were measured on the less dense layers of antibody.