Journal ArticleDOI
The interaction of quercetin with human serum albumin: a fluorescence spectroscopic study.
TLDR
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.About:
This article is published in Biochemical and Biophysical Research Communications.The article was published on 2002-12-06. It has received 201 citations till now. The article focuses on the topics: Fluorescence anisotropy & Human serum albumin.read more
Citations
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Journal ArticleDOI
Flavonoid–serum albumin complexation: determination of binding constants and binding sites by fluorescence spectroscopy
Claire Dufour,Olivier Dangles +1 more
TL;DR: Overall, flavonoids display moderate affinities for albumins (binding constants in the range 1-15 x 10(4) M(-1), flavones and flavonols being most tightly bound), and it can be proposed that the binding of flavonol primarily takes place in subdomain IIA.
Journal ArticleDOI
Interaction of Different Polyphenols with Bovine Serum Albumin (BSA) and Human Salivary α-Amylase (HSA) by Fluorescence Quenching
TL;DR: Fluorescence quenching has proven to be a very sensitive technique with many potentialities to analyze the interaction between polyphenols and proteins because it can detect several interactions that have not been proven by other methods, namely, nephelometry.
Journal ArticleDOI
Molecular spectroscopic study on the interaction of tetracyclines with serum albumins.
TL;DR: A molecular spectroscopic investigation of the interaction between tetracyclines antibiotics and human serum albumin or bovine serumalbumin was reported and the action distances and the energy transfer efficiencies between donor-acceptor were calculated based on the Foster energy transference.
Journal ArticleDOI
Spectroscopic investigation on the interaction of ICT probe 3-acetyl-4-oxo-6,7-dihydro-12H Indolo-[2,3-a] quinolizine with serum albumins.
TL;DR: Micropolarities in the two proteinous environments have been determined following the polarity sensitivity of the CT emission and addition of urea to the protein-bound systems leads to a reduction in the fluorescence anisotropy indicating the denaturation of the proteins.
Journal ArticleDOI
Binding of selected phenolic compounds to proteins.
TL;DR: The structures of the proteins as determined by circular dichroism indicate changes in the tertiary structure with the secondary structure remaining intact.
References
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Book
Principles of fluorescence spectroscopy
TL;DR: This book describes the fundamental aspects of fluorescence, the biochemical applications of this methodology, and the instrumentation used in fluorescence spectroscopy.
Journal ArticleDOI
Excited state proton-transfer spectroscopy of 3-hydroxyflavone and quercetin
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.
Journal ArticleDOI
The Systematic Identification of Flavonoids. Von T. J. Mabry, K. R. Markham und M. B. Thomas. 354 S. mit 325 Abb., Springer-Verlag Berlin – Heidelberg – New York 1970, Preis: DM 98, – (US $ 27.00)
Journal ArticleDOI
Intramolecular excited-state proton transfer in 3-hydroxyflavone. Hydrogen-bonding solvent perturbations
Dale McMorrow,Michael Kasha +1 more
TL;DR: In this article, the phenomenon of excited-state proton transfer in 3-hydroxyflavone is shown to depend sensitively on traces of H-bonding impurities in hydrocarbon solvents.
Related Papers (5)
Flavonoid–serum albumin complexation: determination of binding constants and binding sites by fluorescence spectroscopy
Claire Dufour,Olivier Dangles +1 more