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Human serum albumin and quercetin interactions monitored by time-resolved fluorescence : evidence for enhanced discrete rotamer conformations

Rolinski, O.J. and Martin, A. and Birch, D.J. (2007) Human serum albumin and quercetin interactions monitored by time-resolved fluorescence : evidence for enhanced discrete rotamer conformations. Journal of Biomedical Optics, 12. 034013. ISSN 1083-3668

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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.

Item type: Article
ID code: 9939
Keywords: proteins, molecular biophysics, fluorescence, biochemistry, molecular configurations, radiative lifetimes, rotational isomerism, human serum albumin, tryptophan rotamers, flavonoids, fluorescence lifetime distribution, fluorescence resonance energy transfer, quercetin, Physics
Subjects: Science > Physics
Department: Faculty of Science > Physics
Related URLs:
    Depositing user: Strathprints Administrator
    Date Deposited: 02 Dec 2011 11:30
    Last modified: 12 Mar 2012 10:53
    URI: http://strathprints.strath.ac.uk/id/eprint/9939

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