Drug Binding Properties of Glycosylated Human Serum Albumin as Measured by Fluorescence and Circular Dichroism
Binding properties of Sudlow's site-specific drugs to glycosylated human serum albumin (G-HSA) were investigated using fluorescence and circular dichroism (CD). Dansylamide, phenylbutazone and warfarin were used as site I-specific drugs, and dansylproline, ibuprofen and flufenamic acid were use...
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| Veröffentlicht in: | Biological & pharmaceutical bulletin 1994/01/15, Vol.17(1), pp.16-21 |
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| creator | OKABE, Nobuo HASHIZUME, Noriko |
| description | Binding properties of Sudlow's site-specific drugs to glycosylated human serum albumin (G-HSA) were investigated using fluorescence and circular dichroism (CD). Dansylamide, phenylbutazone and warfarin were used as site I-specific drugs, and dansylproline, ibuprofen and flufenamic acid were used as site II-specific ones. Similar changes in the fluorescence intensity of dansylamide occured in the presence of both G-HSA and intact human serum albumin (HSA), while the fluorescence enhancement of dansylproline caused by G-HSA was extremely weakened in comparison with that by HSA. These results suggest that the glycosylation of HSA inhibits the binding of the site II-specific drug, dansylproline, to HSA, while it does not influence the binding of the site I specific drug, dansylamide. The induced ellipticities of the complexes of ibuprofen, flufenamic acid and phenyl butazone with G-HSA were diminished in comparison with those with HSA. With the complexes of warfarin, the induced ellipticity was enhanced. These CD results suggest that the glycosylation of HSA induces microenvironmental changes in the binding sites for the above site-specific drugs which influence the drug binding ability of HSA. |
| doi_str_mv | 10.1248/bpb.17.16 |
| format | Article |
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Dansylamide, phenylbutazone and warfarin were used as site I-specific drugs, and dansylproline, ibuprofen and flufenamic acid were used as site II-specific ones. Similar changes in the fluorescence intensity of dansylamide occured in the presence of both G-HSA and intact human serum albumin (HSA), while the fluorescence enhancement of dansylproline caused by G-HSA was extremely weakened in comparison with that by HSA. These results suggest that the glycosylation of HSA inhibits the binding of the site II-specific drug, dansylproline, to HSA, while it does not influence the binding of the site I specific drug, dansylamide. The induced ellipticities of the complexes of ibuprofen, flufenamic acid and phenyl butazone with G-HSA were diminished in comparison with those with HSA. With the complexes of warfarin, the induced ellipticity was enhanced. These CD results suggest that the glycosylation of HSA induces microenvironmental changes in the binding sites for the above site-specific drugs which influence the drug binding ability of HSA.</description><identifier>ISSN: 0918-6158</identifier><identifier>EISSN: 1347-5215</identifier><identifier>DOI: 10.1248/bpb.17.16</identifier><identifier>PMID: 8148809</identifier><language>eng</language><publisher>Tokyo: The Pharmaceutical Society of Japan</publisher><subject>Binding Sites ; Biological and medical sciences ; Circular Dichroism ; Dansyl Compounds - metabolism ; drug binding ; Flufenamic Acid - metabolism ; fluorescence ; Fluorescent Dyes - metabolism ; General pharmacology ; glycosylated human serum albumin ; Humans ; Ibuprofen - metabolism ; Medical sciences ; Pharmacokinetics. Pharmacogenetics. Drug-receptor interactions ; Pharmacology. Drug treatments ; Phenylbutazone - metabolism ; Proline - analogs & derivatives ; Proline - metabolism ; Protein Binding ; Serum Albumin - metabolism ; Spectrometry, Fluorescence ; Warfarin - metabolism</subject><ispartof>Biological and Pharmaceutical Bulletin, 1994/01/15, Vol.17(1), pp.16-21</ispartof><rights>The Pharmaceutical Society of Japan</rights><rights>1994 INIST-CNRS</rights><rights>Copyright Japan Science and Technology Agency 1994</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c598t-31b6d1af4f63d69fdb1744b876e7c873afc85bc2ac36e51baa30a66bebf8a0e43</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,1877,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4067786$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8148809$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>OKABE, Nobuo</creatorcontrib><creatorcontrib>HASHIZUME, Noriko</creatorcontrib><title>Drug Binding Properties of Glycosylated Human Serum Albumin as Measured by Fluorescence and Circular Dichroism</title><title>Biological & pharmaceutical bulletin</title><addtitle>Biol Pharm Bull</addtitle><description>Binding properties of Sudlow's site-specific drugs to glycosylated human serum albumin (G-HSA) were investigated using fluorescence and circular dichroism (CD). Dansylamide, phenylbutazone and warfarin were used as site I-specific drugs, and dansylproline, ibuprofen and flufenamic acid were used as site II-specific ones. Similar changes in the fluorescence intensity of dansylamide occured in the presence of both G-HSA and intact human serum albumin (HSA), while the fluorescence enhancement of dansylproline caused by G-HSA was extremely weakened in comparison with that by HSA. These results suggest that the glycosylation of HSA inhibits the binding of the site II-specific drug, dansylproline, to HSA, while it does not influence the binding of the site I specific drug, dansylamide. The induced ellipticities of the complexes of ibuprofen, flufenamic acid and phenyl butazone with G-HSA were diminished in comparison with those with HSA. With the complexes of warfarin, the induced ellipticity was enhanced. These CD results suggest that the glycosylation of HSA induces microenvironmental changes in the binding sites for the above site-specific drugs which influence the drug binding ability of HSA.</description><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Circular Dichroism</subject><subject>Dansyl Compounds - metabolism</subject><subject>drug binding</subject><subject>Flufenamic Acid - metabolism</subject><subject>fluorescence</subject><subject>Fluorescent Dyes - metabolism</subject><subject>General pharmacology</subject><subject>glycosylated human serum albumin</subject><subject>Humans</subject><subject>Ibuprofen - metabolism</subject><subject>Medical sciences</subject><subject>Pharmacokinetics. Pharmacogenetics. Drug-receptor interactions</subject><subject>Pharmacology. Drug treatments</subject><subject>Phenylbutazone - metabolism</subject><subject>Proline - analogs & derivatives</subject><subject>Proline - metabolism</subject><subject>Protein Binding</subject><subject>Serum Albumin - metabolism</subject><subject>Spectrometry, Fluorescence</subject><subject>Warfarin - metabolism</subject><issn>0918-6158</issn><issn>1347-5215</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkU2P0zAQhiMEWroLB34AkiUQEocWu3Zs57jb_UJaBBJwtsbOpOvKcYodH_rvSWnUAxf78Dx6ZzRvVb1jdMXWQn-xe7tiasXki2rBuFDLes3ql9WCNkwvJav16-oy5x2lVNE1v6guNBNa02ZRxdtUtuTGx9bHLfmRhj2m0WMmQ0cewsEN-RBgxJY8lh4i-Ymp9OQ62NL7SCCTbwi5pInbA7kPZUiYHUaHBGJLNj65EiCRW--e0-Bz_6Z61UHI-Hb-r6rf93e_No_Lp-8PXzfXT0tXN3pccmZly6ATneStbLrWMiWE1Uqiclpx6JyurVuD4xJrZgE4BSkt2k4DRcGvqk-n3H0a_hTMo-n9tFgIEHEo2SgpOKUNncQP_4m7oaQ47WaYEA2TlNNj3OeT5dKQc8LO7JPvIR0Mo-bYgJkaMEwZJif3_ZxYbI_t2ZxPPvGPM4fsIHQJovP5rAkqldLHmJuTtssjbPHMYarHBTwOZE3D_w2dH3mG7hmSwcj_AgCYpmA</recordid><startdate>19940101</startdate><enddate>19940101</enddate><creator>OKABE, Nobuo</creator><creator>HASHIZUME, Noriko</creator><general>The Pharmaceutical Society of Japan</general><general>Maruzen</general><general>Japan Science and Technology Agency</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>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19940101</creationdate><title>Drug Binding Properties of Glycosylated Human Serum Albumin as Measured by Fluorescence and Circular Dichroism</title><author>OKABE, Nobuo ; HASHIZUME, Noriko</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c598t-31b6d1af4f63d69fdb1744b876e7c873afc85bc2ac36e51baa30a66bebf8a0e43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Circular Dichroism</topic><topic>Dansyl Compounds - metabolism</topic><topic>drug binding</topic><topic>Flufenamic Acid - metabolism</topic><topic>fluorescence</topic><topic>Fluorescent Dyes - metabolism</topic><topic>General pharmacology</topic><topic>glycosylated human serum albumin</topic><topic>Humans</topic><topic>Ibuprofen - metabolism</topic><topic>Medical sciences</topic><topic>Pharmacokinetics. Pharmacogenetics. Drug-receptor interactions</topic><topic>Pharmacology. Drug treatments</topic><topic>Phenylbutazone - metabolism</topic><topic>Proline - analogs & derivatives</topic><topic>Proline - metabolism</topic><topic>Protein Binding</topic><topic>Serum Albumin - metabolism</topic><topic>Spectrometry, Fluorescence</topic><topic>Warfarin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>OKABE, Nobuo</creatorcontrib><creatorcontrib>HASHIZUME, Noriko</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>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biological & pharmaceutical bulletin</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>OKABE, Nobuo</au><au>HASHIZUME, Noriko</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Drug Binding Properties of Glycosylated Human Serum Albumin as Measured by Fluorescence and Circular Dichroism</atitle><jtitle>Biological & pharmaceutical bulletin</jtitle><addtitle>Biol Pharm Bull</addtitle><date>1994-01-01</date><risdate>1994</risdate><volume>17</volume><issue>1</issue><spage>16</spage><epage>21</epage><pages>16-21</pages><issn>0918-6158</issn><eissn>1347-5215</eissn><abstract>Binding properties of Sudlow's site-specific drugs to glycosylated human serum albumin (G-HSA) were investigated using fluorescence and circular dichroism (CD). Dansylamide, phenylbutazone and warfarin were used as site I-specific drugs, and dansylproline, ibuprofen and flufenamic acid were used as site II-specific ones. Similar changes in the fluorescence intensity of dansylamide occured in the presence of both G-HSA and intact human serum albumin (HSA), while the fluorescence enhancement of dansylproline caused by G-HSA was extremely weakened in comparison with that by HSA. These results suggest that the glycosylation of HSA inhibits the binding of the site II-specific drug, dansylproline, to HSA, while it does not influence the binding of the site I specific drug, dansylamide. The induced ellipticities of the complexes of ibuprofen, flufenamic acid and phenyl butazone with G-HSA were diminished in comparison with those with HSA. With the complexes of warfarin, the induced ellipticity was enhanced. These CD results suggest that the glycosylation of HSA induces microenvironmental changes in the binding sites for the above site-specific drugs which influence the drug binding ability of HSA.</abstract><cop>Tokyo</cop><pub>The Pharmaceutical Society of Japan</pub><pmid>8148809</pmid><doi>10.1248/bpb.17.16</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| source | J-STAGE Free; MEDLINE; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | Binding Sites Biological and medical sciences Circular Dichroism Dansyl Compounds - metabolism drug binding Flufenamic Acid - metabolism fluorescence Fluorescent Dyes - metabolism General pharmacology glycosylated human serum albumin Humans Ibuprofen - metabolism Medical sciences Pharmacokinetics. Pharmacogenetics. Drug-receptor interactions Pharmacology. Drug treatments Phenylbutazone - metabolism Proline - analogs & derivatives Proline - metabolism Protein Binding Serum Albumin - metabolism Spectrometry, Fluorescence Warfarin - metabolism |
| title | Drug Binding Properties of Glycosylated Human Serum Albumin as Measured by Fluorescence and Circular Dichroism |
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