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Journal of Biomedical Optics

Human serum albumin and quercetin interactions monitored by time-resolved fluorescence: evidence for enhanced discrete rotamer conformations
Author(s): Olaf J. Rolinski; Andrew Martin; David J. S. Birch
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Paper 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.

Paper Details

Date Published: 1 May 2007
PDF: 7 pages
J. Biomed. Opt. 12(3) 034013 doi: 10.1117/1.2747623
Published in: Journal of Biomedical Optics Volume 12, Issue 3
Show Author Affiliations
Olaf J. Rolinski, Univ. of Strathclyde (United Kingdom)
Andrew Martin, Univ. of Strathclyde (United Kingdom)
David J. S. Birch, Univ. of Strathclyde (United Kingdom)

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