Comparative Studies on the Interaction of Cochinchinenin A and Loureirin B with Bovine Serum Albumin
This paper describes the simple, sensitive, and effective spectrophotometric methods based on ultraviolet, fluorescence and circular dichroism for revealing the interactional mechanism of Cochinchinenin A (CA) and Loureirin B (LB) with bovine serum albumin (BSA). Under simulated physiological condit...
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| Format: | Article |
| Language: | English |
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Wiley
2013-01-01
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| Series: | Journal of Spectroscopy |
| Online Access: | http://dx.doi.org/10.1155/2013/149615 |
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| author | Tianming Yang Hao Zhang Haiyan Fu Yuanbin She Can Huang Yan Hu Liping Wang |
| author_facet | Tianming Yang Hao Zhang Haiyan Fu Yuanbin She Can Huang Yan Hu Liping Wang |
| author_sort | Tianming Yang |
| collection | DOAJ |
| description | This paper describes the simple, sensitive, and effective spectrophotometric methods based on ultraviolet, fluorescence and circular dichroism for revealing the interactional mechanism of Cochinchinenin A (CA) and Loureirin B (LB) with bovine serum albumin (BSA). Under simulated physiological conditions, it was demonstrated that the fluorescence quenching mechanisms between CA (or LB) and BSA as a static quenching mode, or a combined quenching (dynamic and static quenching) mode were related to concentration level of CA (or LB). The binding distance (rCA, rLB) and the quenching efficiency (KSV), especially for the binding constants value of ligands to BSA, were affected by the methoxyl group at position 4 at different temperatures. The corresponding thermodynamic parameters were also obtained and indicated that electrostatic forces play a major role in the formation of the LB-BSA complex, but probably a combined force for CA-BSA complex. Furthermore, synchronous fluorescence spectroscopy and circular dichroism spectra demonstrated that the secondary structures of BSA were changed to varying degrees by the binding of CA (or LB). |
| format | Article |
| id | doaj-art-390699ce9a7047baac1c584b46d54fee |
| institution | Kabale University |
| issn | 2314-4920 2314-4939 |
| language | English |
| publishDate | 2013-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Journal of Spectroscopy |
| spelling | doaj-art-390699ce9a7047baac1c584b46d54fee2025-02-03T05:46:35ZengWileyJournal of Spectroscopy2314-49202314-49392013-01-01201310.1155/2013/149615149615Comparative Studies on the Interaction of Cochinchinenin A and Loureirin B with Bovine Serum AlbuminTianming Yang0Hao Zhang1Haiyan Fu2Yuanbin She3Can Huang4Yan Hu5Liping Wang6Third Class Laboratory about Ethno-Medicine of State Administration of Traditional Chinese Medicine, College of Pharmacy, South-Central University for Nationalities, Wuhan 430074, ChinaThird Class Laboratory about Ethno-Medicine of State Administration of Traditional Chinese Medicine, College of Pharmacy, South-Central University for Nationalities, Wuhan 430074, ChinaThird Class Laboratory about Ethno-Medicine of State Administration of Traditional Chinese Medicine, College of Pharmacy, South-Central University for Nationalities, Wuhan 430074, ChinaKey Laboratory of Catalysis and Materials Science of the State Ethnic Affairs Commission & Ministry of Education, College of Chemistry and Materials Science, South-Central University for Nationalities, Wuhan 430074, ChinaThird Class Laboratory about Ethno-Medicine of State Administration of Traditional Chinese Medicine, College of Pharmacy, South-Central University for Nationalities, Wuhan 430074, ChinaThird Class Laboratory about Ethno-Medicine of State Administration of Traditional Chinese Medicine, College of Pharmacy, South-Central University for Nationalities, Wuhan 430074, ChinaThird Class Laboratory about Ethno-Medicine of State Administration of Traditional Chinese Medicine, College of Pharmacy, South-Central University for Nationalities, Wuhan 430074, ChinaThis paper describes the simple, sensitive, and effective spectrophotometric methods based on ultraviolet, fluorescence and circular dichroism for revealing the interactional mechanism of Cochinchinenin A (CA) and Loureirin B (LB) with bovine serum albumin (BSA). Under simulated physiological conditions, it was demonstrated that the fluorescence quenching mechanisms between CA (or LB) and BSA as a static quenching mode, or a combined quenching (dynamic and static quenching) mode were related to concentration level of CA (or LB). The binding distance (rCA, rLB) and the quenching efficiency (KSV), especially for the binding constants value of ligands to BSA, were affected by the methoxyl group at position 4 at different temperatures. The corresponding thermodynamic parameters were also obtained and indicated that electrostatic forces play a major role in the formation of the LB-BSA complex, but probably a combined force for CA-BSA complex. Furthermore, synchronous fluorescence spectroscopy and circular dichroism spectra demonstrated that the secondary structures of BSA were changed to varying degrees by the binding of CA (or LB).http://dx.doi.org/10.1155/2013/149615 |
| spellingShingle | Tianming Yang Hao Zhang Haiyan Fu Yuanbin She Can Huang Yan Hu Liping Wang Comparative Studies on the Interaction of Cochinchinenin A and Loureirin B with Bovine Serum Albumin Journal of Spectroscopy |
| title | Comparative Studies on the Interaction of Cochinchinenin A and Loureirin B with Bovine Serum Albumin |
| title_full | Comparative Studies on the Interaction of Cochinchinenin A and Loureirin B with Bovine Serum Albumin |
| title_fullStr | Comparative Studies on the Interaction of Cochinchinenin A and Loureirin B with Bovine Serum Albumin |
| title_full_unstemmed | Comparative Studies on the Interaction of Cochinchinenin A and Loureirin B with Bovine Serum Albumin |
| title_short | Comparative Studies on the Interaction of Cochinchinenin A and Loureirin B with Bovine Serum Albumin |
| title_sort | comparative studies on the interaction of cochinchinenin a and loureirin b with bovine serum albumin |
| url | http://dx.doi.org/10.1155/2013/149615 |
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