Fluorescence Spectroscopy Study on the Interaction between Evodiamine and Bovine Serum Albumin
The interaction of evodiamine (Evo) with bovine serum albumins (BSAs) at different two temperatures (298 and 310 K) was investigated by means of fluorescence spectroscopy. The experimental results showed that Evo binds with BSA via a static quenching procedure with association constants K of 1.61×10...
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| Format: | Article |
| Language: | English |
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Wiley
2013-01-01
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| Series: | Journal of Chemistry |
| Online Access: | http://dx.doi.org/10.1155/2013/308054 |
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| author | Mingxiong Tan Weijiang Liang Xujian Luo Yunqiong Gu |
| author_facet | Mingxiong Tan Weijiang Liang Xujian Luo Yunqiong Gu |
| author_sort | Mingxiong Tan |
| collection | DOAJ |
| description | The interaction of evodiamine (Evo) with bovine serum albumins (BSAs) at different two temperatures (298 and 310 K) was investigated by means of fluorescence spectroscopy. The experimental results showed that Evo binds with BSA via a static quenching procedure with association constants K of 1.61×106 L/mol at 298 K and 6.78×105 L/mol at 310 K. The number of bound Evo molecules per protein is 1.31 at 298 K and 1.33 at 310 K. The results suggested that Evo reacts with BSA chiefly through hydrophobic and electrostatic interactions, and it does not alter the α-helical nature of BAS. |
| format | Article |
| id | doaj-art-905040b392d445368351da7689f3077e |
| institution | Kabale University |
| issn | 2090-9063 2090-9071 |
| language | English |
| publishDate | 2013-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Journal of Chemistry |
| spelling | doaj-art-905040b392d445368351da7689f3077e2025-02-03T01:04:18ZengWileyJournal of Chemistry2090-90632090-90712013-01-01201310.1155/2013/308054308054Fluorescence Spectroscopy Study on the Interaction between Evodiamine and Bovine Serum AlbuminMingxiong Tan0Weijiang Liang1Xujian Luo2Yunqiong Gu3School of Chemistry and Material, Yulin Normal University, Yulin 537000, ChinaSchool of Chemistry and Material, Yulin Normal University, Yulin 537000, ChinaSchool of Chemistry and Material, Yulin Normal University, Yulin 537000, ChinaSchool of Chemistry and Material, Yulin Normal University, Yulin 537000, ChinaThe interaction of evodiamine (Evo) with bovine serum albumins (BSAs) at different two temperatures (298 and 310 K) was investigated by means of fluorescence spectroscopy. The experimental results showed that Evo binds with BSA via a static quenching procedure with association constants K of 1.61×106 L/mol at 298 K and 6.78×105 L/mol at 310 K. The number of bound Evo molecules per protein is 1.31 at 298 K and 1.33 at 310 K. The results suggested that Evo reacts with BSA chiefly through hydrophobic and electrostatic interactions, and it does not alter the α-helical nature of BAS.http://dx.doi.org/10.1155/2013/308054 |
| spellingShingle | Mingxiong Tan Weijiang Liang Xujian Luo Yunqiong Gu Fluorescence Spectroscopy Study on the Interaction between Evodiamine and Bovine Serum Albumin Journal of Chemistry |
| title | Fluorescence Spectroscopy Study on the Interaction between Evodiamine and Bovine Serum Albumin |
| title_full | Fluorescence Spectroscopy Study on the Interaction between Evodiamine and Bovine Serum Albumin |
| title_fullStr | Fluorescence Spectroscopy Study on the Interaction between Evodiamine and Bovine Serum Albumin |
| title_full_unstemmed | Fluorescence Spectroscopy Study on the Interaction between Evodiamine and Bovine Serum Albumin |
| title_short | Fluorescence Spectroscopy Study on the Interaction between Evodiamine and Bovine Serum Albumin |
| title_sort | fluorescence spectroscopy study on the interaction between evodiamine and bovine serum albumin |
| url | http://dx.doi.org/10.1155/2013/308054 |
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