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

O.J. Rolinski; A. Martin; D.J. Birch

doi:10.1117/1.2747623

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

O.J. Rolinski
, A. Martin
, D.J. Birch

Research output: Contribution to journal › Article › peer-review

53 Citations (Scopus)

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 language	English
Journal	Journal of Biomedical Optics
Volume	12
DOIs	https://doi.org/10.1117/1.2747623
Publication status	Published - 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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10.1117/1.2747623

NMS: EPSRC Science and Innovation Nanometrology for Molecular Science, Medicine and Manufacture
Birch, D. (Principal Investigator), Dawson, M. (Co-investigator), Faulds, K. (Co-investigator), Girkin, J. (Co-investigator), Graham, D. (Co-investigator), Martin, R. (Co-investigator), O'Donnell, K. (Co-investigator), Rolinski, O. (Co-investigator), Smith, W. (Co-investigator) & Wynne, K. (Co-investigator)
Scottish Funding Council SFC, EPSRC (Engineering and Physical Sciences Research Council)
1/08/08 → 31/01/12
Project: Research

Cite this

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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 = jun,

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 - evidence for enhanced discrete rotamer conformations

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

SN - 1083-3668

VL - 12

JO - Journal of Biomedical Optics

JF - Journal of Biomedical Optics

ER -

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

Abstract

Keywords

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Projects

NMS: EPSRC Science and Innovation Nanometrology for Molecular Science, Medicine and Manufacture

Cite this