Spectroscopic Studies of the Supramolecular Interactions Between Uracil and 5-Hydroxy-6-Methyluracil with Bovine Serum Albumin and its Bilirubin Complex
Using fluorescence and absorption spectroscopy the interaction of bovine serum albumin and its bilirubin complex with uracil and 5-hydroxy-6-methyluracil in phosphate buffer at pH 7.4 was investigated. The parameters of forming intermolecular complexes (binding constants, quenching rate constants, t...
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| Veröffentlicht in: | The Protein Journal 2013-06, Vol.32 (5), p.343-355 |
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| creator | Solomonov, Alexey V. Rumyantsev, Evgeniy V. Ivanov, Sergey P. Kochergin, Boris A. Antina, Elena V. |
| description | Using fluorescence and absorption spectroscopy the interaction of bovine serum albumin and its bilirubin complex with uracil and 5-hydroxy-6-methyluracil in phosphate buffer at pH 7.4 was investigated. The parameters of forming intermolecular complexes (binding constants, quenching rate constants, the radius of the quenching sphere and etc.) were determined. The interaction between serum albumin and uracils is carried out by the static quenching of protein fluorescence and has predominantly hydrophobic character. Using synchronous fluorescence spectroscopy the influence of uracil and 5-hydroxy-6-methyluracil on the conformational changes of the protein molecule was studied. Uracils effectively binds to bilirubin-albumin complex compared to free protein, which is caused by the interaction with tetrapyrrolic pigment in macromolecular complex. Molecular docking calculations also being presented. |
| doi_str_mv | 10.1007/s10930-013-9493-2 |
| format | Article |
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The parameters of forming intermolecular complexes (binding constants, quenching rate constants, the radius of the quenching sphere and etc.) were determined. The interaction between serum albumin and uracils is carried out by the static quenching of protein fluorescence and has predominantly hydrophobic character. Using synchronous fluorescence spectroscopy the influence of uracil and 5-hydroxy-6-methyluracil on the conformational changes of the protein molecule was studied. Uracils effectively binds to bilirubin-albumin complex compared to free protein, which is caused by the interaction with tetrapyrrolic pigment in macromolecular complex. Molecular docking calculations also being presented.</description><identifier>ISSN: 1572-3887</identifier><identifier>EISSN: 1573-4943</identifier><identifier>EISSN: 1875-8355</identifier><identifier>DOI: 10.1007/s10930-013-9493-2</identifier><identifier>PMID: 23657525</identifier><language>eng</language><publisher>Boston: Springer US</publisher><subject>Absorption spectroscopy ; Albumin ; Animal Anatomy ; Animals ; Bilirubin ; Bilirubin - chemistry ; Biochemistry ; Bioorganic Chemistry ; Cattle ; Chemistry ; Chemistry and Materials Science ; Comparative analysis ; Fluorescence ; Fluorescence spectroscopy ; Histology ; Hydrophobic and Hydrophilic Interactions ; Molecular biology ; Molecular Docking Simulation ; Morphology ; Organic Chemistry ; Phosphates ; Protein Binding ; Proteins ; Pyrimidines ; Serum Albumin, Bovine - chemistry ; Spectrometry, Fluorescence ; Spectrum analysis ; Uracil - analogs & derivatives ; Uracil - chemistry ; X-Ray Absorption Spectroscopy</subject><ispartof>The Protein Journal, 2013-06, Vol.32 (5), p.343-355</ispartof><rights>Springer Science+Business Media New York 2013</rights><rights>COPYRIGHT 2013 Springer</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c439t-12cf86895c6e27612fe6c92afc988b78ae7c925117c85e74bf99bb9fcaccec683</citedby><cites>FETCH-LOGICAL-c439t-12cf86895c6e27612fe6c92afc988b78ae7c925117c85e74bf99bb9fcaccec683</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10930-013-9493-2$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10930-013-9493-2$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27903,27904,41467,42536,51298</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23657525$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Solomonov, Alexey V.</creatorcontrib><creatorcontrib>Rumyantsev, Evgeniy V.</creatorcontrib><creatorcontrib>Ivanov, Sergey P.</creatorcontrib><creatorcontrib>Kochergin, Boris A.</creatorcontrib><creatorcontrib>Antina, Elena V.</creatorcontrib><title>Spectroscopic Studies of the Supramolecular Interactions Between Uracil and 5-Hydroxy-6-Methyluracil with Bovine Serum Albumin and its Bilirubin Complex</title><title>The Protein Journal</title><addtitle>Protein J</addtitle><addtitle>Protein J</addtitle><description>Using fluorescence and absorption spectroscopy the interaction of bovine serum albumin and its bilirubin complex with uracil and 5-hydroxy-6-methyluracil in phosphate buffer at pH 7.4 was investigated. The parameters of forming intermolecular complexes (binding constants, quenching rate constants, the radius of the quenching sphere and etc.) were determined. The interaction between serum albumin and uracils is carried out by the static quenching of protein fluorescence and has predominantly hydrophobic character. Using synchronous fluorescence spectroscopy the influence of uracil and 5-hydroxy-6-methyluracil on the conformational changes of the protein molecule was studied. Uracils effectively binds to bilirubin-albumin complex compared to free protein, which is caused by the interaction with tetrapyrrolic pigment in macromolecular complex. Molecular docking calculations also being presented.</description><subject>Absorption spectroscopy</subject><subject>Albumin</subject><subject>Animal Anatomy</subject><subject>Animals</subject><subject>Bilirubin</subject><subject>Bilirubin - chemistry</subject><subject>Biochemistry</subject><subject>Bioorganic Chemistry</subject><subject>Cattle</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Comparative analysis</subject><subject>Fluorescence</subject><subject>Fluorescence spectroscopy</subject><subject>Histology</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Molecular biology</subject><subject>Molecular Docking Simulation</subject><subject>Morphology</subject><subject>Organic Chemistry</subject><subject>Phosphates</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>Pyrimidines</subject><subject>Serum Albumin, Bovine - chemistry</subject><subject>Spectrometry, Fluorescence</subject><subject>Spectrum analysis</subject><subject>Uracil - 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chemistry</topic><topic>Biochemistry</topic><topic>Bioorganic Chemistry</topic><topic>Cattle</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Comparative analysis</topic><topic>Fluorescence</topic><topic>Fluorescence spectroscopy</topic><topic>Histology</topic><topic>Hydrophobic and Hydrophilic Interactions</topic><topic>Molecular biology</topic><topic>Molecular Docking Simulation</topic><topic>Morphology</topic><topic>Organic Chemistry</topic><topic>Phosphates</topic><topic>Protein Binding</topic><topic>Proteins</topic><topic>Pyrimidines</topic><topic>Serum Albumin, Bovine - chemistry</topic><topic>Spectrometry, Fluorescence</topic><topic>Spectrum analysis</topic><topic>Uracil - analogs & derivatives</topic><topic>Uracil - chemistry</topic><topic>X-Ray Absorption Spectroscopy</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Solomonov, Alexey V.</creatorcontrib><creatorcontrib>Rumyantsev, Evgeniy V.</creatorcontrib><creatorcontrib>Ivanov, Sergey P.</creatorcontrib><creatorcontrib>Kochergin, Boris A.</creatorcontrib><creatorcontrib>Antina, Elena V.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Materials Science Collection</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Protein Journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Solomonov, Alexey V.</au><au>Rumyantsev, Evgeniy V.</au><au>Ivanov, Sergey P.</au><au>Kochergin, Boris A.</au><au>Antina, Elena V.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Spectroscopic Studies of the Supramolecular Interactions Between Uracil and 5-Hydroxy-6-Methyluracil with Bovine Serum Albumin and its Bilirubin Complex</atitle><jtitle>The Protein Journal</jtitle><stitle>Protein J</stitle><addtitle>Protein J</addtitle><date>2013-06-01</date><risdate>2013</risdate><volume>32</volume><issue>5</issue><spage>343</spage><epage>355</epage><pages>343-355</pages><issn>1572-3887</issn><eissn>1573-4943</eissn><eissn>1875-8355</eissn><abstract>Using fluorescence and absorption spectroscopy the interaction of bovine serum albumin and its bilirubin complex with uracil and 5-hydroxy-6-methyluracil in phosphate buffer at pH 7.4 was investigated. The parameters of forming intermolecular complexes (binding constants, quenching rate constants, the radius of the quenching sphere and etc.) were determined. The interaction between serum albumin and uracils is carried out by the static quenching of protein fluorescence and has predominantly hydrophobic character. Using synchronous fluorescence spectroscopy the influence of uracil and 5-hydroxy-6-methyluracil on the conformational changes of the protein molecule was studied. Uracils effectively binds to bilirubin-albumin complex compared to free protein, which is caused by the interaction with tetrapyrrolic pigment in macromolecular complex. Molecular docking calculations also being presented.</abstract><cop>Boston</cop><pub>Springer US</pub><pmid>23657525</pmid><doi>10.1007/s10930-013-9493-2</doi><tpages>13</tpages></addata></record> |
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| subjects | Absorption spectroscopy Albumin Animal Anatomy Animals Bilirubin Bilirubin - chemistry Biochemistry Bioorganic Chemistry Cattle Chemistry Chemistry and Materials Science Comparative analysis Fluorescence Fluorescence spectroscopy Histology Hydrophobic and Hydrophilic Interactions Molecular biology Molecular Docking Simulation Morphology Organic Chemistry Phosphates Protein Binding Proteins Pyrimidines Serum Albumin, Bovine - chemistry Spectrometry, Fluorescence Spectrum analysis Uracil - analogs & derivatives Uracil - chemistry X-Ray Absorption Spectroscopy |
| title | Spectroscopic Studies of the Supramolecular Interactions Between Uracil and 5-Hydroxy-6-Methyluracil with Bovine Serum Albumin and its Bilirubin Complex |
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