FN Archimer Export Format PT J TI Anti-rabbit immunoglobulin G detection in complex medium by PM-RAIRS and QCM Influence of the antibody immobilisation method BT AF BRIAND, Elisabeth SALMAIN, M COMPERE, Chantal PRADIER, C AS 1:1;2:2;3:3;4:1; FF 1:;2:;3:PDG-DOP-DCB-ERT-IC;4:; C1 Univ Paris 06, CNRS, UMR 7609, Lab React Surface, F-75252 Paris 05, France. Ecole Natl Super Chim Paris, UMR 7576, Lab Chim & Biochim Complexes Mol, F-75231 Paris, France. IFREMER, Ctr Brest, Dept Essais & Rech Technol Interfaces & Capteurs, F-29280 Plouzane, France. C2 UNIV PARIS 06, FRANCE ENSCP, FRANCE IFREMER, FRANCE SI BREST SE PDG-DOP-DCB-ERT-MS PDG-DOP-DCB-ERT-IC IN WOS Ifremer jusqu'en 2018 copubli-france copubli-univ-france IF 5.061 TC 39 UR https://archimer.ifremer.fr/doc/2007/publication-3580.pdf LA English DT Article DE ;RIgG immobilisation;PM RAIRS;QCM;Immunosensors AB Two antibody immobilisation procedures were compared to set up an immunosensor for goat anti-rabbit immunoglobulin (anti-rIgG), i.e. rIgG covalently bound or immobilised via affinity to protein A (PrA). In both cases, the first layer of protein was covalently bound to a mixed self-assembled monolayer (SAM) of mercaptoundecanoic acid (MUA) and mercaptohexanol (C6OH) on a gold surface. The elaboration of the sensitive surfaces, as well as their selectivity and sensitivity were studied step by step by polarization modulation-reflection absorption infra-red spectroscopy (PM-RAIRS) and quartz crystal trticrobalance (QCM) with impedance measurement. QCM measurements showed that the viscoelastic properties of the antibody layer were markedly modified during the antigen recognition when the antibody was bound by affinity to PrA. The specific detection of antigen within a complex medium was assessed by PM-RAIRS thanks to the grafting of cobalt-carbonyl probes. Affinity constants between the immobilised rIgG and the anti-rIgG were determined from PM-RAIRS analysis. (c) 2006 Elsevier B.V. All rights reserved. PY 2007 PD JUL SO Biosensors and Bioelectronics SN 0956-5663 PU Elsevier VL 22 IS 12 UT 000247555300017 BP 2884 EP 2890 DI 10.1016/j.bios.2006.12.009 ID 3580 ER EF