Human serum albumin and quercetin interactions monitored by time-resolved fluorescence: evidence for enhanced discrete rotamer conformations.
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.
Rolinski
Olaf J
OJ
University 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
Martin
Andrew
A
Birch
David J S
DJ
D000465:Algorithms; D003198:Computer Simulation; D006801:Humans; D007536:Isomerism; D008856:Microscopy, Fluorescence / Q000379:methods*; D008956:Models, Chemical; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000379:methods*; D011794:Quercetin / Q000737:chemistry*; D012709:Serum Albumin / Q000737:chemistry*
D012709:Serum Albumin; D011794:Quercetin