Pradeep K. Sengupta

TL;DR: In this article, the double minimum hydrogen-bonding potential of 3-hydroxyflavone and quercetin at room temperature in solution has been used to explain the luminescence of these molecules at 77 K in 2-methylbutane rigid matrix.

TL;DR: It is demonstrated that binding of the flavonoids to the RBC membranes significantly inhibits lipid peroxidation, and at the same time enhances their integrity against hypotonic lysis.

TL;DR: The emission, excitation, and anisotropy data indicate that the quercetin molecules bind at a motionally restricted site near tryptophan-214 in the interdomain cleft region of HSA, and the excitation spectrum suggests occurrence of efficient Förster type resonance energy transfer (FRET) from the single tryptophile residue of H SA to the protein bound quercETin.

TL;DR: Analysis of relevant spectroscopic data leads to the conclusions that two binding sites are involved in BSA–3HF interaction, and the interaction is slightly positively cooperative in nature with a similar binding constant.

TL;DR: The novel use of the intrinsic fluorescence characteristics of the plant flavonoid fisetin (3,3′,4′,7‐OH flavone) to explore its binding and site(s) of solubilisation in egg lecithin liposomal membranes is demonstrated.