1 May 2007 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.
© (2007) Society of Photo-Optical Instrumentation Engineers (SPIE)
Olaf J. Rolinski, Olaf J. Rolinski, Andrew Martin, Andrew Martin, David J. S. Birch, David J. S. Birch, } "Human serum albumin and quercetin interactions monitored by time-resolved fluorescence: evidence for enhanced discrete rotamer conformations," Journal of Biomedical Optics 12(3), 034013 (1 May 2007). https://doi.org/10.1117/1.2747623 . Submission:
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