Immobilization of Protein A on SAMS for the elaboration of immunosensors
| Type | Article | ||||||||
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| Date | 2006-12 | ||||||||
| Language | English | ||||||||
| Author(s) | Briand Elisabeth1, Salmain Michèle2, Compere Chantal 3, Pradier Claire-Marie1 |
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| Affiliation(s) | 1 : Univ Paris 06, CNRS, UMR 7609, Lab React Surface, F-75005 Paris, France. 2 : Ecole Natl Super Chim Paris, CNRS, UMR 7576, Lab Chim & Biochim Complexes Mol, F-75231 Paris 05, France. 3 : IFREMER, Serv Interfaces & Capteurs, F-29280 Plouzane, France. |
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| Source | Colloids and Surfaces B: Biointerfaces (0927-7765) (Elsevier), 2006-12 , Vol. 53 , N. 2 , P. 215-224 | ||||||||
| DOI | 10.1016/j.colsurfb.2006.09.010 | ||||||||
| WOS© Times Cited | 90 | ||||||||
| Keyword(s) | PM IRRAS, Antibody, Protein A, Gold, Self assembled monolayers | ||||||||
| Abstract | Binary mixtures of 11-mercaptoundecanoic acid (MUA) and other thiols of various lengths and terminal functions were chemisorbed on gold-coated surfaces via S-Au bonds to form mixed self-assembled monolayers (SAMs). Several values of the inole fraction of MUA in the thiol mixtures were tested and the structure and composition of the resulted thin films were characterized by X-ray photoelectron spectroscopy (XPS) and polarization modulation infrared reflection-absorption spectroscopy (PM-IRRAS). The results made it clear that co-adsorption of MUA with thiols of similar chain length led to well-ordered monolayers whereas the co-adsorption of MUA with shorter thiols yielded less crystalline-like thin films, but with more reactive carboxylic acid terminal groups. This criterion appeared decisive for efficient covalent binding of Stapkylococcus aureus Protein A (PrA), a protein that displays high affinity for the constant fragment (Fc) of antibodies of the IgG type from various mammal species. The ability of immobilized Protein A to recognize and bind a model IgG appeared to be optimal for the mixed SAM of MUA and the short-chain, omega-hydroxythiot 6-mercaptohexanol in the proportion 1-3. (c) 2006 Elsevier B.V. All rights reserved. | ||||||||
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