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. ISSN 1083-3668 (https://doi.org/10.1117/1.2747623)

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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.

ORCID iDs

Rolinski, O.J. ORCID logoORCID: https://orcid.org/0000-0002-7838-779X, Martin, A. and Birch, D.J. ORCID logoORCID: https://orcid.org/0000-0001-6400-1270;
  • Item type:Article
    ID code:9939
    Dates:
    Date
    Event
    15 June 2007
    Published
    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, Biomedical Engineering, Biomaterials, Electronic, Optical and Magnetic Materials, Atomic and Molecular Physics, and Optics
    Subjects:Science > Physics
    Department:Faculty of Science > Physics
    Depositing user: Strathprints Administrator
    Date deposited:02 Dec 2011 11:30
    Last modified:19 May 2023 01:23
    URI:https://strathprints.strath.ac.uk/id/eprint/9939
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