Surface-bound biomembranes incorporating receptors: electrochemical and structural characterization
A generic method is described for forming surface-bound structures that incorporate protein receptors in a membrane-like environment. Silane reagents (octadecyltrichlorosilane and dimethyloctadecylchlorosilane) were used to produce primed substrates bearing full and partial monolayers, respectively....
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Veröffentlicht in: | Biosensors & bioelectronics 1992, Vol.7 (6), p.429-440 |
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creator | Downer, Nancy W. Jianguo, Li Penniman, Elizabeth M. DeLuca, Leslie W. Smith, H.Gilbert |
description | A generic method is described for forming surface-bound structures that incorporate protein receptors in a membrane-like environment. Silane reagents (octadecyltrichlorosilane and dimethyloctadecylchlorosilane) were used to produce primed substrates bearing full and partial monolayers, respectively. Biomembranes were formed by dialysis of detergent-solubilized membranes in the presence of two different alkylsilanized substrates: Si/SiO
2 electrodes and glass microspheres. Electrochemical analysis of the capacitance was used to determine apparent thickness and degree of surface coverage at each stage in the deposition process. Elemental analysis on glass beads gave the hydrocarbon incorporation. Glass bead substrates were also examined by Fourier transform infrared spectroscopy to evaluate the alkylsilanized substrate before and after dialysis. Both vertebrate rhodopsin and the nicotinic acetylcholine receptor could be incorporated into structures with composition and dimensions similar to natural bilayer membranes. The techniques reported here are applicable for coupling membrane receptors to a variety of transducing substrates used in biosensors. |
doi_str_mv | 10.1016/0956-5663(92)85042-9 |
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2 electrodes and glass microspheres. Electrochemical analysis of the capacitance was used to determine apparent thickness and degree of surface coverage at each stage in the deposition process. Elemental analysis on glass beads gave the hydrocarbon incorporation. Glass bead substrates were also examined by Fourier transform infrared spectroscopy to evaluate the alkylsilanized substrate before and after dialysis. Both vertebrate rhodopsin and the nicotinic acetylcholine receptor could be incorporated into structures with composition and dimensions similar to natural bilayer membranes. The techniques reported here are applicable for coupling membrane receptors to a variety of transducing substrates used in biosensors.</description><identifier>ISSN: 0956-5663</identifier><identifier>EISSN: 1873-4235</identifier><identifier>DOI: 10.1016/0956-5663(92)85042-9</identifier><identifier>PMID: 1325158</identifier><language>eng</language><publisher>Lausanne: Elsevier B.V</publisher><subject>acetylcholine receptor ; Animals ; Biological and medical sciences ; biomembrane ; Biosensing Techniques ; Biotechnology ; Electrochemistry ; Evaluation Studies as Topic ; FTIR ; Fundamental and applied biological sciences. Psychology ; membrane reconsitution ; Membranes - chemistry ; Membranes - metabolism ; Methods. Procedures. Technologies ; Molecular Structure ; Others ; Phospholipids - chemistry ; Phospholipids - metabolism ; receptor ; Receptors, Cell Surface - chemistry ; Receptors, Cell Surface - metabolism ; Receptors, Nicotinic - chemistry ; Receptors, Nicotinic - metabolism ; rhodopsin ; Rhodopsin - chemistry ; Rhodopsin - metabolism ; Spectrophotometry, Infrared ; Various methods and equipments</subject><ispartof>Biosensors & bioelectronics, 1992, Vol.7 (6), p.429-440</ispartof><rights>1992</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c448t-7fd8f1137e670b1c307bdd8e47f0a849de56e69fc09cf4b3736f94a6080e4a063</citedby><cites>FETCH-LOGICAL-c448t-7fd8f1137e670b1c307bdd8e47f0a849de56e69fc09cf4b3736f94a6080e4a063</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0956566392850429$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,4010,27902,27903,27904,65308</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5402133$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1325158$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Downer, Nancy W.</creatorcontrib><creatorcontrib>Jianguo, Li</creatorcontrib><creatorcontrib>Penniman, Elizabeth M.</creatorcontrib><creatorcontrib>DeLuca, Leslie W.</creatorcontrib><creatorcontrib>Smith, H.Gilbert</creatorcontrib><title>Surface-bound biomembranes incorporating receptors: electrochemical and structural characterization</title><title>Biosensors & bioelectronics</title><addtitle>Biosens Bioelectron</addtitle><description>A generic method is described for forming surface-bound structures that incorporate protein receptors in a membrane-like environment. Silane reagents (octadecyltrichlorosilane and dimethyloctadecylchlorosilane) were used to produce primed substrates bearing full and partial monolayers, respectively. Biomembranes were formed by dialysis of detergent-solubilized membranes in the presence of two different alkylsilanized substrates: Si/SiO
2 electrodes and glass microspheres. Electrochemical analysis of the capacitance was used to determine apparent thickness and degree of surface coverage at each stage in the deposition process. Elemental analysis on glass beads gave the hydrocarbon incorporation. Glass bead substrates were also examined by Fourier transform infrared spectroscopy to evaluate the alkylsilanized substrate before and after dialysis. Both vertebrate rhodopsin and the nicotinic acetylcholine receptor could be incorporated into structures with composition and dimensions similar to natural bilayer membranes. The techniques reported here are applicable for coupling membrane receptors to a variety of transducing substrates used in biosensors.</description><subject>acetylcholine receptor</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>biomembrane</subject><subject>Biosensing Techniques</subject><subject>Biotechnology</subject><subject>Electrochemistry</subject><subject>Evaluation Studies as Topic</subject><subject>FTIR</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>membrane reconsitution</subject><subject>Membranes - chemistry</subject><subject>Membranes - metabolism</subject><subject>Methods. Procedures. Technologies</subject><subject>Molecular Structure</subject><subject>Others</subject><subject>Phospholipids - chemistry</subject><subject>Phospholipids - metabolism</subject><subject>receptor</subject><subject>Receptors, Cell Surface - chemistry</subject><subject>Receptors, Cell Surface - metabolism</subject><subject>Receptors, Nicotinic - chemistry</subject><subject>Receptors, Nicotinic - metabolism</subject><subject>rhodopsin</subject><subject>Rhodopsin - chemistry</subject><subject>Rhodopsin - metabolism</subject><subject>Spectrophotometry, Infrared</subject><subject>Various methods and equipments</subject><issn>0956-5663</issn><issn>1873-4235</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU2LFDEQhoMo67j6DxT6IKKH1krnq7MHQRa_YMGDeg7p6oob6e6MSbegv96MM6w39VSEet6iUg9jDzk858D1C7BKt0pr8dR2z3oFsmvtLbbjvRGt7IS6zXY3yF12r5SvAGC4hTN2xkWnuOp3DD9uOXikdkjbMjZDTDPNQ_YLlSYumPI-Zb_G5UuTCWm_plwuGpoI15zwmuaIfmp8TZY1b7huuT7x2mePK-X4s0bTcp_dCX4q9OBUz9nnN68_Xb5rrz68fX_56qpFKfu1NWHsA-fCkDYwcBRghnHsSZoAvpd2JKVJ24BgMchBGKGDlV5DDyQ9aHHOnhzn7nP6tlFZ3RwL0jTV36StOCO4sZ2Bf4Jca2Wl1v8BCqUA-grKI4g5lZIpuH2Os88_HAd3sOUOKtxBhbOd-23L2Rp7dJq_DTONf0JHPbX_-NT3pR46VC8Yyw2mJHRciIq9PGJUr_s9UnYFIy1IY6zWVjem-Pc9fgErzbJV</recordid><startdate>1992</startdate><enddate>1992</enddate><creator>Downer, Nancy W.</creator><creator>Jianguo, Li</creator><creator>Penniman, Elizabeth M.</creator><creator>DeLuca, Leslie W.</creator><creator>Smith, H.Gilbert</creator><general>Elsevier B.V</general><general>Elsevier Science</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>1992</creationdate><title>Surface-bound biomembranes incorporating receptors: electrochemical and structural characterization</title><author>Downer, Nancy W. ; Jianguo, Li ; Penniman, Elizabeth M. ; DeLuca, Leslie W. ; Smith, H.Gilbert</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c448t-7fd8f1137e670b1c307bdd8e47f0a849de56e69fc09cf4b3736f94a6080e4a063</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>acetylcholine receptor</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>biomembrane</topic><topic>Biosensing Techniques</topic><topic>Biotechnology</topic><topic>Electrochemistry</topic><topic>Evaluation Studies as Topic</topic><topic>FTIR</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>membrane reconsitution</topic><topic>Membranes - chemistry</topic><topic>Membranes - metabolism</topic><topic>Methods. Procedures. Technologies</topic><topic>Molecular Structure</topic><topic>Others</topic><topic>Phospholipids - chemistry</topic><topic>Phospholipids - metabolism</topic><topic>receptor</topic><topic>Receptors, Cell Surface - chemistry</topic><topic>Receptors, Cell Surface - metabolism</topic><topic>Receptors, Nicotinic - chemistry</topic><topic>Receptors, Nicotinic - metabolism</topic><topic>rhodopsin</topic><topic>Rhodopsin - chemistry</topic><topic>Rhodopsin - metabolism</topic><topic>Spectrophotometry, Infrared</topic><topic>Various methods and equipments</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Downer, Nancy W.</creatorcontrib><creatorcontrib>Jianguo, Li</creatorcontrib><creatorcontrib>Penniman, Elizabeth M.</creatorcontrib><creatorcontrib>DeLuca, Leslie W.</creatorcontrib><creatorcontrib>Smith, H.Gilbert</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biosensors & bioelectronics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Downer, Nancy W.</au><au>Jianguo, Li</au><au>Penniman, Elizabeth M.</au><au>DeLuca, Leslie W.</au><au>Smith, H.Gilbert</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Surface-bound biomembranes incorporating receptors: electrochemical and structural characterization</atitle><jtitle>Biosensors & bioelectronics</jtitle><addtitle>Biosens Bioelectron</addtitle><date>1992</date><risdate>1992</risdate><volume>7</volume><issue>6</issue><spage>429</spage><epage>440</epage><pages>429-440</pages><issn>0956-5663</issn><eissn>1873-4235</eissn><abstract>A generic method is described for forming surface-bound structures that incorporate protein receptors in a membrane-like environment. Silane reagents (octadecyltrichlorosilane and dimethyloctadecylchlorosilane) were used to produce primed substrates bearing full and partial monolayers, respectively. Biomembranes were formed by dialysis of detergent-solubilized membranes in the presence of two different alkylsilanized substrates: Si/SiO
2 electrodes and glass microspheres. Electrochemical analysis of the capacitance was used to determine apparent thickness and degree of surface coverage at each stage in the deposition process. Elemental analysis on glass beads gave the hydrocarbon incorporation. Glass bead substrates were also examined by Fourier transform infrared spectroscopy to evaluate the alkylsilanized substrate before and after dialysis. Both vertebrate rhodopsin and the nicotinic acetylcholine receptor could be incorporated into structures with composition and dimensions similar to natural bilayer membranes. The techniques reported here are applicable for coupling membrane receptors to a variety of transducing substrates used in biosensors.</abstract><cop>Lausanne</cop><pub>Elsevier B.V</pub><pmid>1325158</pmid><doi>10.1016/0956-5663(92)85042-9</doi><tpages>12</tpages></addata></record> |
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subjects | acetylcholine receptor Animals Biological and medical sciences biomembrane Biosensing Techniques Biotechnology Electrochemistry Evaluation Studies as Topic FTIR Fundamental and applied biological sciences. Psychology membrane reconsitution Membranes - chemistry Membranes - metabolism Methods. Procedures. Technologies Molecular Structure Others Phospholipids - chemistry Phospholipids - metabolism receptor Receptors, Cell Surface - chemistry Receptors, Cell Surface - metabolism Receptors, Nicotinic - chemistry Receptors, Nicotinic - metabolism rhodopsin Rhodopsin - chemistry Rhodopsin - metabolism Spectrophotometry, Infrared Various methods and equipments |
title | Surface-bound biomembranes incorporating receptors: electrochemical and structural characterization |
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