Changes of serum albumin affinity for aspirin induced by fatty acid

被引：43

作者：

Bojko, B. ^{[1
]}

Sulkowska, A. ^{[1
]}

Maciazek, M. ^{[1
]}

Rownicka, J. ^{[1
]}

Njau, F. ^{[1
]}

Sulkowski, W. W. ^{[2
]}

机构：

[1] L Warynski Silesian Med Acad, Fac Pharm, Dept Phys Pharm, Sosnowiec, Poland

[2] Silesian Univ, Dept Environm Chem & Technol, Inst Chem, Katowice, Poland

来源：

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2008年 / 42卷 / 04期

关键词：

aspirin; fatty acid; albumin; binding; quenching fluorescence method;

D O I：

10.1016/j.ijbiomac.2007.11.002

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (c) 2008 Published by Elsevier B.V.

引用

页码：314 / 323

页数：10

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