Journal
JOURNAL OF LUMINESCENCE
Volume 151, Issue -, Pages 219-223Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jlumin.2014.02.028
Keywords
Antithyroid drug; Methimazole; Human serum albumin; Fluorescence spectroscopy; Isothermal titration calorimetry
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Funding
- Council of Scientific and Industrial Research (CSIR), New Delhi, India
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The interaction of the anti-thyroid drug, 2-mercapto 1-methylimidazole (methimazole) with human serum albumin (HSA) has been examined by fluorescence and isothermal titration calorimetry (ITC) techniques. Fluorescence results indicate that in case of HSA-drug complex the quenching of fluorescence intensity is at 340 nm. The methimazole has an ability to quench the intrinsic fluorescence of HSA tryptophan through a static quenching procedure. The binding constant has been determined using Stern-Volmer modified equation and energy transfer mechanisms of quenching are discussed. The Delta G degrees, Delta H degrees, and Delta S degrees values are also calculated by ITC measurements. The experimental spectroscopic and thermodynamic parameters have been used for understanding the binding mechanism of anti-thyroid drug with HSA. (C) 2014 Elsevier B.V. All rights reserved.
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