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

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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.
Original languageEnglish
JournalJournal of Biomedical Optics
Volume12
DOIs
Publication statusPublished - 15 Jun 2007

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

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