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    • Keywords


      Human serum albumin; bovine serum albumin; quercetin; energy transfer; binding constant

    • Abstract


      Binding of quercetin to human serum albumin (HSA) was studied and the binding constant measured by following the red-shifted absorption spectrum of quercetin in the presence of HSA and the quenching of the intrinsic protein fluorescence in the presence of different concentrations of quercetin. Fluorescence lifetime measurements of HSA showed decrease in the average lifetimes indicating binding at a location, near the tryptophan moiety, and the possibility of fluorescence energy transfer between excited tryptophan and quercetin. Critical transfer distance (Ro) was determined, from which the mean distance between tryptophan-214 in HSA and quercetin was calculated. The above studies were also carried out with bovine serum albumin (BSA).

    • Author Affiliations


      Beena Mishra1 Atanu Barik1 K Indira Priyadarsini1 Hari Mohan1

      1. Radiation Chemistry & Chemical Dynamics Division, Bhabha Atomic Research Centre, Trombay, Mumbai - 400 085, India
    • Dates

  • Journal of Chemical Sciences | News

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