Spectroscopic Studies and Life Time Measurements of Binding of a Bioactive Compound to Bovine Serum Albumin and the Effects of Common Ions and Other Drugs on Binding
The mechanism of binding of anti-inflammatory drug, nimesulide (NIM) with bovine serum albumin (BSA) was investigated by fluorescence, absorption, circular dichroism (CD) and lifetime measurements under simulative physiological conditions. The analysis of fluorescence data indicated the presence of...
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| Veröffentlicht in: | Chemical & Pharmaceutical Bulletin 2006, Vol.54(4), pp.422-427 |
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| creator | Shaikh, Sarfaraj Mohd Takhi Seetharamappa, Jaldappa Ashoka, Siddaramanna Kandagal, Pradeep Basavaraj |
| description | The mechanism of binding of anti-inflammatory drug, nimesulide (NIM) with bovine serum albumin (BSA) was investigated by fluorescence, absorption, circular dichroism (CD) and lifetime measurements under simulative physiological conditions. The analysis of fluorescence data indicated the presence of both dynamic and static quenching mechanism in the binding. Various binding parameters have been evaluated. The CD spectral data revealed the decrease in α-helical content of BSA from 70.9% (in free BSA) to 42.03% (in bound form) thereby indicating the conformational change in BSA upon binding. The binding of NIM to BSA was also confirmed by absorption spectra. Based on the Förster's theory of non-radiation energy transfer, the binding average distance, r between the donor (BSA) and acceptor (NIM) was found to be 2.17 nm. The association constants of NIM-BSA decreased in presence of the common ions and other drugs thereby indicating the availability of higher concentration of free drug (NIM) in plasma. |
| doi_str_mv | 10.1248/cpb.54.422 |
| format | Article |
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The analysis of fluorescence data indicated the presence of both dynamic and static quenching mechanism in the binding. Various binding parameters have been evaluated. The CD spectral data revealed the decrease in α-helical content of BSA from 70.9% (in free BSA) to 42.03% (in bound form) thereby indicating the conformational change in BSA upon binding. The binding of NIM to BSA was also confirmed by absorption spectra. Based on the Förster's theory of non-radiation energy transfer, the binding average distance, r between the donor (BSA) and acceptor (NIM) was found to be 2.17 nm. The association constants of NIM-BSA decreased in presence of the common ions and other drugs thereby indicating the availability of higher concentration of free drug (NIM) in plasma.</description><identifier>ISSN: 0009-2363</identifier><identifier>EISSN: 1347-5223</identifier><identifier>DOI: 10.1248/cpb.54.422</identifier><identifier>PMID: 16595938</identifier><language>eng</language><publisher>Japan: The Pharmaceutical Society of Japan</publisher><subject>Animals ; Anti-Inflammatory Agents, Non-Steroidal - analysis ; Anti-Inflammatory Agents, Non-Steroidal - metabolism ; anti-inflammatory drug ; Binding Sites ; bovine serum albumin ; Cattle ; Circular Dichroism - methods ; Drug Interactions ; Ions - chemistry ; Serum Albumin, Bovine - analysis ; Serum Albumin, Bovine - metabolism ; Spectrometry, Fluorescence - methods ; Spectrophotometry, Ultraviolet - methods ; spectroscopic study ; Sulfonamides - analysis ; Sulfonamides - metabolism ; Technology, Pharmaceutical - methods</subject><ispartof>Chemical and Pharmaceutical Bulletin, 2006, Vol.54(4), pp.422-427</ispartof><rights>2006 The Pharmaceutical Society of Japan</rights><rights>Copyright Japan Science and Technology Agency 2006</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c685t-c0694cb6f2b03e7afc1662f691ffa8a8a2052d069fbbfdc46ad2bc1595c1fc613</citedby><cites>FETCH-LOGICAL-c685t-c0694cb6f2b03e7afc1662f691ffa8a8a2052d069fbbfdc46ad2bc1595c1fc613</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,1877,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16595938$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shaikh, Sarfaraj Mohd Takhi</creatorcontrib><creatorcontrib>Seetharamappa, Jaldappa</creatorcontrib><creatorcontrib>Ashoka, Siddaramanna</creatorcontrib><creatorcontrib>Kandagal, Pradeep Basavaraj</creatorcontrib><creatorcontrib>Karnatak University</creatorcontrib><creatorcontrib>Department of Chemistry</creatorcontrib><title>Spectroscopic Studies and Life Time Measurements of Binding of a Bioactive Compound to Bovine Serum Albumin and the Effects of Common Ions and Other Drugs on Binding</title><title>Chemical & Pharmaceutical Bulletin</title><addtitle>Chem. Pharm. Bull.</addtitle><description>The mechanism of binding of anti-inflammatory drug, nimesulide (NIM) with bovine serum albumin (BSA) was investigated by fluorescence, absorption, circular dichroism (CD) and lifetime measurements under simulative physiological conditions. The analysis of fluorescence data indicated the presence of both dynamic and static quenching mechanism in the binding. Various binding parameters have been evaluated. The CD spectral data revealed the decrease in α-helical content of BSA from 70.9% (in free BSA) to 42.03% (in bound form) thereby indicating the conformational change in BSA upon binding. The binding of NIM to BSA was also confirmed by absorption spectra. Based on the Förster's theory of non-radiation energy transfer, the binding average distance, r between the donor (BSA) and acceptor (NIM) was found to be 2.17 nm. The association constants of NIM-BSA decreased in presence of the common ions and other drugs thereby indicating the availability of higher concentration of free drug (NIM) in plasma.</description><subject>Animals</subject><subject>Anti-Inflammatory Agents, Non-Steroidal - analysis</subject><subject>Anti-Inflammatory Agents, Non-Steroidal - metabolism</subject><subject>anti-inflammatory drug</subject><subject>Binding Sites</subject><subject>bovine serum albumin</subject><subject>Cattle</subject><subject>Circular Dichroism - methods</subject><subject>Drug Interactions</subject><subject>Ions - chemistry</subject><subject>Serum Albumin, Bovine - analysis</subject><subject>Serum Albumin, Bovine - metabolism</subject><subject>Spectrometry, Fluorescence - methods</subject><subject>Spectrophotometry, Ultraviolet - methods</subject><subject>spectroscopic study</subject><subject>Sulfonamides - analysis</subject><subject>Sulfonamides - metabolism</subject><subject>Technology, Pharmaceutical - methods</subject><issn>0009-2363</issn><issn>1347-5223</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFUV1v0zAUjRCIlcELPwBZ4m1Sir-TPKGtjDGpaA8dz5bj2K2rxg52MokfxP_kdimdLN1r65x7jnVPUXwkeEkor7-YoV0KvuSUvioWhPGqFJSy18UCY9yUlEl2UbzLeY8xFbhib4sLIkUjGlYvir-bwZoxxWzi4A3ajFPnbUY6dGjtnUWPvrfop9V5Sra3YcwoOnTjQ-fD9njV8IjajP7JolXshzjB5BjRTXzywaKNTVOPrg_t1PvwrDruLLp1DkyfpWCmjwHdxzCbPgCe0Lc0bQEO_53eF2-cPmT74dQvi1_fbx9XP8r1w9396npdGlmLsTRYNty00tEWM1tpZ4iU1MmGOKdrOBQL2gHJta3rDJe6o60hsAtDnJGEXRafZ90hxd-TzaPaxykFsFSES8zqStAGWFczy8DecrJODcn3Ov1RBKtjIgoSUYIrSATIn06SU9vb7oV6igAIdzMBUG_0IYYDbO7F2OTK7GzvFcVYKowFxxwaUxjkj6UiuKql4KD0dVba51Fv7dlKp9Gbgz3_ai7H6TOy00nZwP4BgLu1kw</recordid><startdate>20060401</startdate><enddate>20060401</enddate><creator>Shaikh, Sarfaraj Mohd Takhi</creator><creator>Seetharamappa, Jaldappa</creator><creator>Ashoka, Siddaramanna</creator><creator>Kandagal, Pradeep Basavaraj</creator><general>The Pharmaceutical Society of Japan</general><general>Pharmaceutical Society of Japan</general><general>Japan Science and Technology Agency</general><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>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>H94</scope></search><sort><creationdate>20060401</creationdate><title>Spectroscopic Studies and Life Time Measurements of Binding of a Bioactive Compound to Bovine Serum Albumin and the Effects of Common Ions and Other Drugs on Binding</title><author>Shaikh, Sarfaraj Mohd Takhi ; Seetharamappa, Jaldappa ; Ashoka, Siddaramanna ; Kandagal, Pradeep Basavaraj</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c685t-c0694cb6f2b03e7afc1662f691ffa8a8a2052d069fbbfdc46ad2bc1595c1fc613</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Animals</topic><topic>Anti-Inflammatory Agents, Non-Steroidal - analysis</topic><topic>Anti-Inflammatory Agents, Non-Steroidal - metabolism</topic><topic>anti-inflammatory drug</topic><topic>Binding Sites</topic><topic>bovine serum albumin</topic><topic>Cattle</topic><topic>Circular Dichroism - methods</topic><topic>Drug Interactions</topic><topic>Ions - chemistry</topic><topic>Serum Albumin, Bovine - analysis</topic><topic>Serum Albumin, Bovine - metabolism</topic><topic>Spectrometry, Fluorescence - methods</topic><topic>Spectrophotometry, Ultraviolet - methods</topic><topic>spectroscopic study</topic><topic>Sulfonamides - analysis</topic><topic>Sulfonamides - metabolism</topic><topic>Technology, Pharmaceutical - methods</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shaikh, Sarfaraj Mohd Takhi</creatorcontrib><creatorcontrib>Seetharamappa, Jaldappa</creatorcontrib><creatorcontrib>Ashoka, Siddaramanna</creatorcontrib><creatorcontrib>Kandagal, Pradeep Basavaraj</creatorcontrib><creatorcontrib>Karnatak University</creatorcontrib><creatorcontrib>Department of Chemistry</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><jtitle>Chemical & Pharmaceutical Bulletin</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shaikh, Sarfaraj Mohd Takhi</au><au>Seetharamappa, Jaldappa</au><au>Ashoka, Siddaramanna</au><au>Kandagal, Pradeep Basavaraj</au><aucorp>Karnatak University</aucorp><aucorp>Department of Chemistry</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Spectroscopic Studies and Life Time Measurements of Binding of a Bioactive Compound to Bovine Serum Albumin and the Effects of Common Ions and Other Drugs on Binding</atitle><jtitle>Chemical & Pharmaceutical Bulletin</jtitle><addtitle>Chem. Pharm. Bull.</addtitle><date>2006-04-01</date><risdate>2006</risdate><volume>54</volume><issue>4</issue><spage>422</spage><epage>427</epage><pages>422-427</pages><issn>0009-2363</issn><eissn>1347-5223</eissn><abstract>The mechanism of binding of anti-inflammatory drug, nimesulide (NIM) with bovine serum albumin (BSA) was investigated by fluorescence, absorption, circular dichroism (CD) and lifetime measurements under simulative physiological conditions. The analysis of fluorescence data indicated the presence of both dynamic and static quenching mechanism in the binding. Various binding parameters have been evaluated. The CD spectral data revealed the decrease in α-helical content of BSA from 70.9% (in free BSA) to 42.03% (in bound form) thereby indicating the conformational change in BSA upon binding. The binding of NIM to BSA was also confirmed by absorption spectra. Based on the Förster's theory of non-radiation energy transfer, the binding average distance, r between the donor (BSA) and acceptor (NIM) was found to be 2.17 nm. The association constants of NIM-BSA decreased in presence of the common ions and other drugs thereby indicating the availability of higher concentration of free drug (NIM) in plasma.</abstract><cop>Japan</cop><pub>The Pharmaceutical Society of Japan</pub><pmid>16595938</pmid><doi>10.1248/cpb.54.422</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Anti-Inflammatory Agents, Non-Steroidal - analysis Anti-Inflammatory Agents, Non-Steroidal - metabolism anti-inflammatory drug Binding Sites bovine serum albumin Cattle Circular Dichroism - methods Drug Interactions Ions - chemistry Serum Albumin, Bovine - analysis Serum Albumin, Bovine - metabolism Spectrometry, Fluorescence - methods Spectrophotometry, Ultraviolet - methods spectroscopic study Sulfonamides - analysis Sulfonamides - metabolism Technology, Pharmaceutical - methods |
| title | Spectroscopic Studies and Life Time Measurements of Binding of a Bioactive Compound to Bovine Serum Albumin and the Effects of Common Ions and Other Drugs on Binding |
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