Changes of serum albumin affinity for aspirin induced by fatty acid

• Published in: International journal of biological macromolecules Vol. 42; no. 4; pp. 314 - 323
• Main Authors: Bojko, B., Sułkowska, A., Maciążek, M., Równicka, J., Njau, F., Sułkowski, W.W.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.05.2008
• Subjects: Albumin; Albumins - chemistry; Animals; Anticoagulants - pharmacology; Aspirin; Aspirin - chemistry; Aspirin - pharmacology; Binding; Binding Sites; Cattle; Fatty acid; Fatty Acids - chemistry; Humans; Hydrogen-Ion Concentration; Kinetics; Ligands; Myristic Acid - chemistry; Protein Binding; Quenching fluorescence method; Serum Albumin - metabolism; Tryptophan - chemistry; Binding; Albumin; Aspirin; Quenching fluorescence method; Fatty acid
• ISSN: 0141-8130; 1879-0003
• DOI: 10.1016/j.ijbiomac.2007.11.002

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.