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Updated: Jul 13, 2026
A Rapid and Quantitative Fluorimetric Method for Protein-Targeting Small Molecule Drug Screening
Published on: October 16, 2015
Human serum albumin and quercetin interactions monitored by time-resolved fluorescence: evidence for enhanced
Olaf J Rolinski1, Andrew Martin, David J S Birch
1University of Strathclyde, Scottish Universities Physics Alliance, Photophysics Group, Department of Physics, John Anderson Building, 107 Rottenrow, Glasgow G4 0NG, United Kingdom. o.j.rolinski@strath.ac.uk
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.
