Abstract
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.
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This work was financially supported by UEFISCDI Romania, Project PCE-2011-3-0032.
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Bogdan, M., Floare, C.G., Pirnau, A. et al. Competitive Binding of Tolmetin to β-Cyclodextrin and Human Serum Albumin: 1H NMR and Fluorescence Spectroscopy Studies. J Solution Chem 46, 44–57 (2017). https://doi.org/10.1007/s10953-016-0549-8
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DOI: https://doi.org/10.1007/s10953-016-0549-8