A quartz crystal resonant sensor (QCRS) study of HSA-drug interactions
Human serum albumin (HSA) was immobilised on the gold surface of a quartz crystal resonance sensor (QCRS) and exposed to warfarin and diazepam. Distinct decreases in frequency of differing magnitudes were observed upon exposure of the protein to each of the compounds suggesting strongly that a ligan...
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Veröffentlicht in: | Analyst (London) 2001-04, Vol.126 (4), p.426-428 |
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creator | PAVEY, Karl D LYLE, A. Emma-Louise OLLIFF, Cedric J PAUL, Frank |
description | Human serum albumin (HSA) was immobilised on the gold surface of a quartz crystal resonance sensor (QCRS) and exposed to warfarin and diazepam. Distinct decreases in frequency of differing magnitudes were observed upon exposure of the protein to each of the compounds suggesting strongly that a ligand interaction was occurring. Moreover, as sequential exposure in any order was observed to yield distinct repeatable frequency decreases for the ligands indicated, screening for site specific binding may be possible. Identically immobilised bovine serum albumin (BSA) gave no response to either compound. |
doi_str_mv | 10.1039/b009986o |
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Emma-Louise ; OLLIFF, Cedric J ; PAUL, Frank</creator><creatorcontrib>PAVEY, Karl D ; LYLE, A. Emma-Louise ; OLLIFF, Cedric J ; PAUL, Frank</creatorcontrib><description>Human serum albumin (HSA) was immobilised on the gold surface of a quartz crystal resonance sensor (QCRS) and exposed to warfarin and diazepam. Distinct decreases in frequency of differing magnitudes were observed upon exposure of the protein to each of the compounds suggesting strongly that a ligand interaction was occurring. Moreover, as sequential exposure in any order was observed to yield distinct repeatable frequency decreases for the ligands indicated, screening for site specific binding may be possible. Identically immobilised bovine serum albumin (BSA) gave no response to either compound.</description><identifier>ISSN: 0003-2654</identifier><identifier>EISSN: 1364-5528</identifier><identifier>DOI: 10.1039/b009986o</identifier><identifier>PMID: 11340971</identifier><identifier>CODEN: ANALAO</identifier><language>eng</language><publisher>Cambridge: Royal Society of Chemistry</publisher><subject>Animals ; Anticoagulants - metabolism ; Binding Sites ; Biological and medical sciences ; Cattle ; Diazepam - metabolism ; Flow Injection Analysis ; General pharmacology ; Gold ; Humans ; Hypnotics and Sedatives - metabolism ; Medical sciences ; Oscillometry - methods ; Pharmacokinetics. Pharmacogenetics. Drug-receptor interactions ; Pharmacology. Drug treatments ; Protein Binding ; Quartz ; quartz crystal resonance sensor ; Serum Albumin - metabolism ; Serum Albumin, Bovine - metabolism ; warfarin ; Warfarin - metabolism</subject><ispartof>Analyst (London), 2001-04, Vol.126 (4), p.426-428</ispartof><rights>2001 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c339t-e72b89fab9c89a0f497e9003a641fb93e0c81e0ace2a597b15a97559ad4ed8aa3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,2818,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1039586$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11340971$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>PAVEY, Karl D</creatorcontrib><creatorcontrib>LYLE, A. Emma-Louise</creatorcontrib><creatorcontrib>OLLIFF, Cedric J</creatorcontrib><creatorcontrib>PAUL, Frank</creatorcontrib><title>A quartz crystal resonant sensor (QCRS) study of HSA-drug interactions</title><title>Analyst (London)</title><addtitle>Analyst</addtitle><description>Human serum albumin (HSA) was immobilised on the gold surface of a quartz crystal resonance sensor (QCRS) and exposed to warfarin and diazepam. Distinct decreases in frequency of differing magnitudes were observed upon exposure of the protein to each of the compounds suggesting strongly that a ligand interaction was occurring. Moreover, as sequential exposure in any order was observed to yield distinct repeatable frequency decreases for the ligands indicated, screening for site specific binding may be possible. Identically immobilised bovine serum albumin (BSA) gave no response to either compound.</description><subject>Animals</subject><subject>Anticoagulants - metabolism</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Cattle</subject><subject>Diazepam - metabolism</subject><subject>Flow Injection Analysis</subject><subject>General pharmacology</subject><subject>Gold</subject><subject>Humans</subject><subject>Hypnotics and Sedatives - metabolism</subject><subject>Medical sciences</subject><subject>Oscillometry - methods</subject><subject>Pharmacokinetics. Pharmacogenetics. Drug-receptor interactions</subject><subject>Pharmacology. Drug treatments</subject><subject>Protein Binding</subject><subject>Quartz</subject><subject>quartz crystal resonance sensor</subject><subject>Serum Albumin - metabolism</subject><subject>Serum Albumin, Bovine - metabolism</subject><subject>warfarin</subject><subject>Warfarin - metabolism</subject><issn>0003-2654</issn><issn>1364-5528</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0EFLwzAUB_AgiptT8BNIDiLzUE2apk2OYzgnDESn5_KaplLpmpmXHuant7KK3jw9Hvz4v8efkHPObjgT-rZgTGuVugMy5iJNIiljdUjGjDERxalMRuQE8b1fOZPsmIw4FwnTGR-TxYx-dODDJzV-hwEa6i26FtpA0bboPJ0-zZ_X1xRDV-6oq-hyPYtK373Rug3Wgwm1a_GUHFXQoD0b5oS8Lu5e5sto9Xj_MJ-tIiOEDpHN4kLpCgptlAZWJTqzun8S0oRXhRaWGcUtA2NjkDoruASdSamhTGypAMSEXO1zt959dBZDvqnR2KaB1roO84ypmMdc_gt5prRUXPVwuofGO0Rvq3zr6w34Xc5Z_l1u_lNuTy-GzK7Y2PIXDm324HIAgAaaykNravwTKPqbqfgCL5h_5g</recordid><startdate>20010401</startdate><enddate>20010401</enddate><creator>PAVEY, Karl D</creator><creator>LYLE, A. 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Drug treatments</topic><topic>Protein Binding</topic><topic>Quartz</topic><topic>quartz crystal resonance sensor</topic><topic>Serum Albumin - metabolism</topic><topic>Serum Albumin, Bovine - metabolism</topic><topic>warfarin</topic><topic>Warfarin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>PAVEY, Karl D</creatorcontrib><creatorcontrib>LYLE, A. Emma-Louise</creatorcontrib><creatorcontrib>OLLIFF, Cedric J</creatorcontrib><creatorcontrib>PAUL, Frank</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>Toxicology Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Analyst (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>PAVEY, Karl D</au><au>LYLE, A. Emma-Louise</au><au>OLLIFF, Cedric J</au><au>PAUL, Frank</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A quartz crystal resonant sensor (QCRS) study of HSA-drug interactions</atitle><jtitle>Analyst (London)</jtitle><addtitle>Analyst</addtitle><date>2001-04-01</date><risdate>2001</risdate><volume>126</volume><issue>4</issue><spage>426</spage><epage>428</epage><pages>426-428</pages><issn>0003-2654</issn><eissn>1364-5528</eissn><coden>ANALAO</coden><abstract>Human serum albumin (HSA) was immobilised on the gold surface of a quartz crystal resonance sensor (QCRS) and exposed to warfarin and diazepam. Distinct decreases in frequency of differing magnitudes were observed upon exposure of the protein to each of the compounds suggesting strongly that a ligand interaction was occurring. Moreover, as sequential exposure in any order was observed to yield distinct repeatable frequency decreases for the ligands indicated, screening for site specific binding may be possible. Identically immobilised bovine serum albumin (BSA) gave no response to either compound.</abstract><cop>Cambridge</cop><pub>Royal Society of Chemistry</pub><pmid>11340971</pmid><doi>10.1039/b009986o</doi><tpages>3</tpages></addata></record> |
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source | Royal Society of Chemistry Journals Archive (1841-2007); MEDLINE; Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection |
subjects | Animals Anticoagulants - metabolism Binding Sites Biological and medical sciences Cattle Diazepam - metabolism Flow Injection Analysis General pharmacology Gold Humans Hypnotics and Sedatives - metabolism Medical sciences Oscillometry - methods Pharmacokinetics. Pharmacogenetics. Drug-receptor interactions Pharmacology. Drug treatments Protein Binding Quartz quartz crystal resonance sensor Serum Albumin - metabolism Serum Albumin, Bovine - metabolism warfarin Warfarin - metabolism |
title | A quartz crystal resonant sensor (QCRS) study of HSA-drug interactions |
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