Competitive Binding of Tolmetin to β-Cyclodextrin and Human Serum Albumin: ¹H NMR and Fluorescence Spectroscopy Studies

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• 作者：M. Bogdan ; C. G. Floare ; A. Pirnau ; S. Neamtu
• 关键词：Tolmetin ; β ; Cyclodextrin ; Human serum albumin ; Binding constants ; NMR spectroscopy ; Fluorescence spectroscopy
• 刊名：Journal of Solution Chemistry
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：46
• 期：1
• 页码：44-57
• 全文大小：
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Physical Chemistry; Industrial Chemistry/Chemical Engineering; Geochemistry; Oceanography; Inorganic Chemistry; Condensed Matter Physics;
• 出版者：Springer US
• ISSN：1572-8927
• 卷排序：46

文摘

The host–guest interaction of tolmetin (TOL) with β-cyclodextrin (β-CD) and the influence of human serum albumin (HSA) on the formation of the inclusion complex were studied by 1D and 2D NMR spectroscopy. The TOL/β-CD inclusion complex formed at a molar ratio of 1:1 with a binding constant value of 2164.5 L·mol−1. Data analysis showed that the addition of 10 μmol·L−1 of HSA weakened the strength of TOL binding to β-CD (K_a = 1493 L·mol−1). The interaction of TOL with HSA in the absence and presence of β-CD was studied by analyzing the fluorescence quenching data. The Stern–Volmer quenching constants and the binding constants are found to be smaller in the presence of β-CD, suggesting that β-CD hinders the strong interaction of TOL with HSA by complex formation. Additionally, the presence of β-CD does not induce conformational and microenvironmental changes on HSA.