Changes of serum albumin affinity for aspirin induced by fatty acid

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 resul...

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Published inInternational 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
LanguageEnglish
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
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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.
AbstractList 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.
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.
Author Sułkowska, A.
Bojko, B.
Sułkowski, W.W.
Równicka, J.
Njau, F.
Maciążek, M.
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  surname: Bojko
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  surname: Równicka
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  surname: Sułkowski
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  organization: Department of Environmental Chemistry and Technology, Institute of Chemistry, University of Silesia, Katowice, Poland
BackLink https://www.ncbi.nlm.nih.gov/pubmed/18346781$$D View this record in MEDLINE/PubMed
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Keywords Binding
Albumin
Aspirin
Quenching fluorescence method
Fatty acid
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Snippet Saturated fatty acids such as myristic acid play an important role in the pathogenesis of cardiovascular disorders. Using the quenching fluorescence method we...
Saturated fatty acids such as myristic acid play an important role in the pathogenesis of cardiovascular disorders. Using the quenching fluorescence method we...
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StartPage 314
SubjectTerms 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
Title Changes of serum albumin affinity for aspirin induced by fatty acid
URI https://dx.doi.org/10.1016/j.ijbiomac.2007.11.002
https://www.ncbi.nlm.nih.gov/pubmed/18346781
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