Journal
JOURNAL OF LUMINESCENCE
Volume 129, Issue 3, Pages 169-175Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jlumin.2008.09.008
Keywords
Methyl blue; Human serum albumin; Fluorescence spectroscopy; Energy transfer
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Funding
- National Science Foundation of China [20875059]
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The interaction of methyl blue (MB) with human serum albumin (HSA) was studied by fluorescence and absorption spectroscopy. The intrinsic fluorescence of HSA was quenched by MB, which was rationalized in terms of the static quenching mechanism. The number of binding sites and the apparent binding constants at different temperatures were obtained from the Stern-Volmer analysis of the fluorescence quenching data. The thermodynamic parameters determined by the van't Hoff analysis of the binding constants (Delta H degrees = 39.8 kJ mol(-1) and Delta S degrees = 239 J mol(-1) K-1) clearly indicate that binding is absolutely entropy-driven and enthalpically disfavored The efficiency of energy transfer and the distance between the donor (HSA) and the acceptor (MB) were calculated as 60% and 2.06 rim, from the Forster theory of non-radiation energy transfer. (C) 2008 Elsevier B.V. All rights reserved.
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