Interaction of Avelox with Bovine Serum Albumin and Effect of the Coexistent Drugs on the Reaction
The interaction between Avelox and bovine serum albumin (BSA) was investigated at different temperatures by fluorescence spectroscopy. Results showed that Avelox could quench the intrinsic fluorescence of BSA strongly, and the quenching mechanism was a static quenching process with Förester spectros...
Saved in:
| Main Authors: | , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Wiley
2012-01-01
|
| Series: | International Journal of Analytical Chemistry |
| Online Access: | http://dx.doi.org/10.1155/2012/408057 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1850158251483594752 |
|---|---|
| author | Baosheng Liu Chao Yang Xiaona Yan Jing Wang Yunkai Lv |
| author_facet | Baosheng Liu Chao Yang Xiaona Yan Jing Wang Yunkai Lv |
| author_sort | Baosheng Liu |
| collection | DOAJ |
| description | The interaction between Avelox and bovine serum albumin (BSA) was investigated at different temperatures by fluorescence spectroscopy. Results showed that Avelox could quench the intrinsic fluorescence of BSA strongly, and the quenching mechanism was a static quenching process with Förester spectroscopy energy transfer. The electrostatic force played an important role on the conjugation reaction between BSA and Avelox. The order of magnitude of binding constants (Ka) was 104, and the number of binding site (n) in the binary system was approximately equal to 1. The binding distance (r) was less than 3 nm and the primary binding site for Avelox was located in subdomain IIA of BSA. Synchronous fluorescence spectra clearly revealed that the microenvironment of amino acid residues and the conformation of BSA were changed during the binding reaction. In addition, the effect of some antibiotics on the binding constant of Avelox with BSA was also studied. |
| format | Article |
| id | doaj-art-69b01815e40f4a87a1b59bb9415a618b |
| institution | OA Journals |
| issn | 1687-8760 1687-8779 |
| language | English |
| publishDate | 2012-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | International Journal of Analytical Chemistry |
| spelling | doaj-art-69b01815e40f4a87a1b59bb9415a618b2025-08-20T02:23:56ZengWileyInternational Journal of Analytical Chemistry1687-87601687-87792012-01-01201210.1155/2012/408057408057Interaction of Avelox with Bovine Serum Albumin and Effect of the Coexistent Drugs on the ReactionBaosheng Liu0Chao Yang1Xiaona Yan2Jing Wang3Yunkai Lv4Key Laboratory of Medical Chemistry and Molecular Diagnosis, College of Chemistry & Environmental Science, Hebei University, Ministry of Education, Baoding 071002, ChinaKey Laboratory of Medical Chemistry and Molecular Diagnosis, College of Chemistry & Environmental Science, Hebei University, Ministry of Education, Baoding 071002, ChinaKey Laboratory of Medical Chemistry and Molecular Diagnosis, College of Chemistry & Environmental Science, Hebei University, Ministry of Education, Baoding 071002, ChinaKey Laboratory of Medical Chemistry and Molecular Diagnosis, College of Chemistry & Environmental Science, Hebei University, Ministry of Education, Baoding 071002, ChinaKey Laboratory of Medical Chemistry and Molecular Diagnosis, College of Chemistry & Environmental Science, Hebei University, Ministry of Education, Baoding 071002, ChinaThe interaction between Avelox and bovine serum albumin (BSA) was investigated at different temperatures by fluorescence spectroscopy. Results showed that Avelox could quench the intrinsic fluorescence of BSA strongly, and the quenching mechanism was a static quenching process with Förester spectroscopy energy transfer. The electrostatic force played an important role on the conjugation reaction between BSA and Avelox. The order of magnitude of binding constants (Ka) was 104, and the number of binding site (n) in the binary system was approximately equal to 1. The binding distance (r) was less than 3 nm and the primary binding site for Avelox was located in subdomain IIA of BSA. Synchronous fluorescence spectra clearly revealed that the microenvironment of amino acid residues and the conformation of BSA were changed during the binding reaction. In addition, the effect of some antibiotics on the binding constant of Avelox with BSA was also studied.http://dx.doi.org/10.1155/2012/408057 |
| spellingShingle | Baosheng Liu Chao Yang Xiaona Yan Jing Wang Yunkai Lv Interaction of Avelox with Bovine Serum Albumin and Effect of the Coexistent Drugs on the Reaction International Journal of Analytical Chemistry |
| title | Interaction of Avelox with Bovine Serum Albumin and Effect of the Coexistent Drugs on the Reaction |
| title_full | Interaction of Avelox with Bovine Serum Albumin and Effect of the Coexistent Drugs on the Reaction |
| title_fullStr | Interaction of Avelox with Bovine Serum Albumin and Effect of the Coexistent Drugs on the Reaction |
| title_full_unstemmed | Interaction of Avelox with Bovine Serum Albumin and Effect of the Coexistent Drugs on the Reaction |
| title_short | Interaction of Avelox with Bovine Serum Albumin and Effect of the Coexistent Drugs on the Reaction |
| title_sort | interaction of avelox with bovine serum albumin and effect of the coexistent drugs on the reaction |
| url | http://dx.doi.org/10.1155/2012/408057 |
| work_keys_str_mv | AT baoshengliu interactionofaveloxwithbovineserumalbuminandeffectofthecoexistentdrugsonthereaction AT chaoyang interactionofaveloxwithbovineserumalbuminandeffectofthecoexistentdrugsonthereaction AT xiaonayan interactionofaveloxwithbovineserumalbuminandeffectofthecoexistentdrugsonthereaction AT jingwang interactionofaveloxwithbovineserumalbuminandeffectofthecoexistentdrugsonthereaction AT yunkailv interactionofaveloxwithbovineserumalbuminandeffectofthecoexistentdrugsonthereaction |