Detecting Conformational Rotamers via TCSPC

Detecting Conformational Rotamers via TCSPC

Among the possible fluorescence biosensors for medical and biochemical monitoring and imaging are the flavonoids, compounds that occur in many plants and their products, such as tea, chocolate, and red wine. Flavonoids recently have intrigued biologists, for they act as antioxidants in cancer and other diseases related to free radicals. Flavonoids bind to nucleic acids and proteins. Many flavonoids, like proteins, are fluorescent, thus setting thestage for experiments involving Förster resonance energy-transfer  (FRET) between the two types of compounds when they bind together. Dr. Olaf Rolinski and Professor David Birch, at the University of Strathclyde in Scotland, have investigated complexation of the protein human serum albumin (HSA, Fig. 1) with the flavonoid quercetin (Q, Fig. 2), using time-domain fluorescence spectroscopy. 1


1 O.J. Rolinski, et al., “Human Serum Albumin and quercetin interactions monitored by time-resolved fluorescence: evidence for enhanced discrete rotamer conformations,” J. Biomed. Optics, 12(3), 034013, 2007.

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