Spectroscopic analysis of the binding interaction between tinidazole and Bovine Serum Albumin (BSA) Journal Article
| Authors: | Shi, X. Y.; Cao, H.; Ren, F. L.; Xu, M. |
| Article Title: | Spectroscopic analysis of the binding interaction between tinidazole and Bovine Serum Albumin (BSA) |
| Abstract: | The interaction between bovine serum albumin (BSA) and tinidazole (Tindamax®; 1) in aqueous solution was investigated in detail by means of UV/VIS and fluorescence spectroscopy, as well as through resonance light-scattering (RLS) spectroscopy. The apparent binding constant and number of binding sites were determined at three different temperatures, as well as the average binding distances between 1 and the nearest amino acid residue(s) of BSA, as analyzed by means of Förster's theory of non-radiation energy transfer. Compound 1 was found to quench the inner fluorescence of BSA by forming a tight 1: 1 aggregate, based on both static quenching and non-radiation energy transfer. The entropy change upon complexation was positive, and the enthalpy change was negative, indicating that the observed spontaneous binding is mainly driven by electrostatic interactions. © 2007 Verlag Helvetica Chimica Acta AG, Zürich. |
| Keywords: | nonhuman; binding affinity; animals; energy transfer; binding site; temperature; amino acid; solutions; thermodynamics; binding sites; fluorescence spectroscopy; bovine serum albumin; cattle; molecular structure; serum albumin, bovine; spectroscopy; aqueous solution; drug protein binding; theory; spectrum analysis; bovinae; ultraviolet spectroscopy; chemical interaction; light scattering; tinidazole; nonphotochemical quenching |
| Journal Title: | Chemistry & Biodiversity |
| Volume: | 4 |
| Issue: | 12 |
| ISSN: | 1612-1872 |
| Publisher: | John Wiley & Sons |
| Date Published: | 2007-12-01 |
| Start Page: | 2780 |
| End Page: | 2790 |
| Language: | English |
| DOI: | 10.1002/cbdv.200790227 |
| PUBMED: | 18081088 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | --- - "Cited By (since 1996): 2" - "Export Date: 17 November 2011" - "Source: Scopus" |
