Immobilization of Protein A on SAMs for the elaboration of immunosensors
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 mole fraction of MUA in the thiol mixtures were tested and the...
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| Veröffentlicht in: | Colloids and surfaces 2006-12, Vol.53 (2), p.215-224 |
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| creator | Briand, Elisabeth Salmain, Michèle Compère, Chantal Pradier, Claire-Marie |
| description | 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 mole 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
Staphylococcus 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, ω-hydroxythiol 6-mercaptohexanol in the proportion 1–3. |
| doi_str_mv | 10.1016/j.colsurfb.2006.09.010 |
| format | Article |
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Staphylococcus 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, ω-hydroxythiol 6-mercaptohexanol in the proportion 1–3.</description><identifier>ISSN: 0927-7765</identifier><identifier>ISSN: 0166-6622</identifier><identifier>EISSN: 1873-4367</identifier><identifier>EISSN: 1873-4340</identifier><identifier>DOI: 10.1016/j.colsurfb.2006.09.010</identifier><identifier>PMID: 17056235</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Antibody ; Catalysis ; Chemical Sciences ; Fatty Acids - chemistry ; Fatty Acids - metabolism ; Gold ; Gold - chemistry ; Immunoglobulin G - metabolism ; Material chemistry ; PM-IRRAS ; Protein A ; Self-assembled monolayers ; Spectroscopy, Fourier Transform Infrared ; Staphylococcal Protein A - chemistry ; Staphylococcal Protein A - metabolism ; Staphylococcus aureus ; Sulfhydryl Compounds - chemistry ; Sulfhydryl Compounds - metabolism</subject><ispartof>Colloids and surfaces, 2006-12, Vol.53 (2), p.215-224</ispartof><rights>2006 Elsevier B.V.</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c545t-3361a7003fd7b0f7bd8606c37ab3ca0bf1e12826e9f57010b2493231199dcc883</citedby><cites>FETCH-LOGICAL-c545t-3361a7003fd7b0f7bd8606c37ab3ca0bf1e12826e9f57010b2493231199dcc883</cites><orcidid>0000-0003-3039-5659</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.colsurfb.2006.09.010$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,885,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17056235$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-00111187$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Briand, Elisabeth</creatorcontrib><creatorcontrib>Salmain, Michèle</creatorcontrib><creatorcontrib>Compère, Chantal</creatorcontrib><creatorcontrib>Pradier, Claire-Marie</creatorcontrib><title>Immobilization of Protein A on SAMs for the elaboration of immunosensors</title><title>Colloids and surfaces</title><addtitle>Colloids Surf B Biointerfaces</addtitle><description>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 mole 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
Staphylococcus 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. 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Several values of the mole 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
Staphylococcus 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, ω-hydroxythiol 6-mercaptohexanol in the proportion 1–3.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>17056235</pmid><doi>10.1016/j.colsurfb.2006.09.010</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0003-3039-5659</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Antibody Catalysis Chemical Sciences Fatty Acids - chemistry Fatty Acids - metabolism Gold Gold - chemistry Immunoglobulin G - metabolism Material chemistry PM-IRRAS Protein A Self-assembled monolayers Spectroscopy, Fourier Transform Infrared Staphylococcal Protein A - chemistry Staphylococcal Protein A - metabolism Staphylococcus aureus Sulfhydryl Compounds - chemistry Sulfhydryl Compounds - metabolism |
| title | Immobilization of Protein A on SAMs for the elaboration of immunosensors |
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