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)

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: https://orcid.org/0000-0002-7838-779X

Birch, D.J. ORCID: https://orcid.org/0000-0001-6400-1270

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• Item metadata

  Item type:	Article
  ID code:	9939
  Dates:	Date Event 15 June 2007 Published
  Subjects:	Science > Physics
  Department:	Faculty of Science > Physics
  Depositing user:	Strathprints Administrator
  Date deposited:	02 Dec 2011 11:30
  Last modified:	11 Nov 2024 09:01
  URI:	https://strathprints.strath.ac.uk/id/eprint/9939