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Study on the interaction between methyl blue and human serum albumin by fluorescence spectrometry
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 co...
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Published in: | Journal of luminescence 2009-03, Vol.129 (3), p.169-175 |
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Main Authors: | , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | 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 (Δ
H°=39.8
kJ
mol
−1 and Δ
S°=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
nm from the Förster theory of non-radiation energy transfer. |
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ISSN: | 0022-2313 1872-7883 |
DOI: | 10.1016/j.jlumin.2008.09.008 |