1 May 2007 Human serum albumin and quercetin interactions monitored by time-resolved fluorescence: evidence for enhanced discrete rotamer conformations
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J. of Biomedical Optics, 12(3), 034013 (2007). doi:10.1117/1.2747623
Abstract
Human serum albumin (HSA) complexation with quercetin, a flavonoid commonly present in human diet, was monitored by means of fluorescence decays of the single HSA tryptophan - Trp214. Data analysis based on fitting to multiexponential functions and determining the lifetime distributions revealed a high sensitivity of tryptophan fluorescence to binding quercetin. Results are discussed in terms of the rotamer model for tryptophan, HSA-quercetin complexation and potential HSA to quercetin energy transfer. Evidence for quercetin stabilising tryptophan rotamers in HSA is presented.
Olaf J. Rolinski, Andrew Martin, David J. S. Birch, "Human serum albumin and quercetin interactions monitored by time-resolved fluorescence: evidence for enhanced discrete rotamer conformations," Journal of Biomedical Optics 12(3), 034013 (1 May 2007). http://dx.doi.org/10.1117/1.2747623
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KEYWORDS
Luminescence

Absorption

Fluorescence resonance energy transfer

Molecules

Proteins

Time resolved spectroscopy

Fluorescence spectroscopy

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