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Changes of serum albumin affinity for aspirin induced by fatty acid |
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| Authors: | Bojko B Sułkowska A Maciazek M Równicka J Njau F Sułkowski W W |
| Affiliation: | aDepartment of Physical Pharmacy, Faculty of Pharmacy, Medical University of Silesia, Sosnowiec, Poland bDepartment of Environmental Chemistry and Technology, Institute of Chemistry, University of Silesia, Katowice, Poland |
| Abstract: | Saturated fatty acids such as myristic acid play an important role in the pathogenesis of cardiovascular disorders. Using the quenching fluorescence method we examined the influence of myristate on the changes of transporting protein affinity towards aspirin—the most popular anticoagulant. Our results showed that the presence of the myristic acid alters the stability of the anticoagulant–albumin complex. The ranges of [myristate]/[albumin] molar ratio at which the stability of drug–protein complex increases or decreases were determined. The differences in interaction between ligands and human or bovine serum albumins were identified. The competition in binding of ligands with these albumins was also described. |
| Keywords: | Aspirin Fatty acid Albumin Binding Quenching fluorescence method |
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