| Autor: |
Kandagal PB; Department of Chemistry, Karnatak University, Dharwad, India., Seetharamappa J, Ashoka S, Shaikh SM, Manjunatha DH |
| Jazyk: |
angličtina |
| Zdroj: |
International journal of biological macromolecules [Int J Biol Macromol] 2006 Nov 15; Vol. 39 (4-5), pp. 234-9. Date of Electronic Publication: 2006 Apr 01. |
| DOI: |
10.1016/j.ijbiomac.2006.03.027 |
| Abstrakt: |
The binding of doxepin hydrochloride (DH) to bovine serum albumin (BSA) was investigated by spectroscopic (fluorescence, UV-vis absorption and circular dichroism) techniques. The binding parameters have been evaluated by fluorescence quenching method. The thermodynamic parameters, Delta H major, Delta S major, and Delta G major calculated at different temperatures indicated that the hydrogen bond and hydrophobic forces played a major role in the interaction of DH with BSA. Based on the Förster's theory of non-radiation energy transfer, the binding average distance, r between the donor (BSA) and acceptor (DH) was evaluated and found to be 2.7 nm. Spectral results observed showed that the binding of DH to BSA induced conformational changes in BSA. The effect of common ions on the binding of DH to BSA was also examined. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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