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

Fingerprint

Quercetin
Complexation
albumins
Serum Albumin
serums
tryptophan
Conformations
Tryptophan
Fluorescence
Flavonoids
fluorescence
Nutrition
Energy transfer
interactions
diets
energy transfer
life (durability)
sensitivity
decay

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

Cite this

@article{0d092b6923ae403c9ab9106bd6d0a8ab,
title = "Human serum albumin and quercetin interactions monitored by time-resolved fluorescence: evidence for enhanced discrete rotamer conformations",
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.",
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",
author = "O.J. Rolinski and A. Martin and D.J. Birch",
year = "2007",
month = "6",
day = "15",
doi = "10.1117/1.2747623",
language = "English",
volume = "12",
journal = "Journal of Biomedical Optics",
issn = "1083-3668",

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TY - JOUR

T1 - Human serum albumin and quercetin interactions monitored by time-resolved fluorescence

T2 - Journal of Biomedical Optics

AU - Rolinski, O.J.

AU - Martin, A.

AU - Birch, D.J.

PY - 2007/6/15

Y1 - 2007/6/15

N2 - 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.

AB - 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.

KW - proteins

KW - molecular biophysics

KW - fluorescence

KW - biochemistry

KW - molecular configurations

KW - radiative lifetimes

KW - rotational isomerism

KW - human serum albumin

KW - tryptophan rotamers

KW - flavonoids

KW - fluorescence lifetime distribution

KW - fluorescence resonance energy transfer

KW - quercetin

U2 - 10.1117/1.2747623

DO - 10.1117/1.2747623

M3 - Article

VL - 12

JO - Journal of Biomedical Optics

JF - Journal of Biomedical Optics

SN - 1083-3668

ER -