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Effect of Denaturating Agents on the Structural Alterations and Drug-Binding Capacity of Human and Bovine Serum Albumin |
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| Authors: | J. Równicka-Zubik A. Sułkowska M. Maciążek-Jurczyk L. Sułkowski W. W. Sułkowski |
| Affiliation: | 1. Department of Physical Pharmacy , Medical University of Silesia , Jagiellońska , Sosnowiec , Poland jrownicka@sum.edu.pl;3. Department of Physical Pharmacy , Medical University of Silesia , Jagiellońska , Sosnowiec , Poland;4. Department of General and Vascular Surgery with Polytrauma Sub-Department , Regional Specialistic Hospital , Czestochowa , Poland;5. Department of Environmental Chemistry and Technology , Institute of Chemistry, University of Silesia , Szkolna , Katowice , Poland |
| Abstract: | Sulindac (SDC) is a nonsteroidal anti-inflammatory drug, useful in the treatment of chronic and acute inflammatory conditions. The binding of SDC to human serum albumin and bovine serum albumin was studied by fluorescence spectroscopy and the results compared with those obtained for human and bovine serum albumin destabilized with urea and guanidine hydrochloride. SDC interacts with serum albumin within the hydrophobic subdomain IIA and/or IB. The analysis of the binding constants shows that the studied albumins preserve their binding capacity in the presence of destabilizing/denaturating agents. The denaturation coefficient has been calculated to estimate the degree of denaturation of protein. |
| Keywords: | bovine serum albumin denaturation fluorescence quenching human serum albumin sulindac |