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Protein-flavonol interaction: fluorescence spectroscopic study
- Source :
- Proteins. 43(2)
- Publication Year :
- 2001
-
Abstract
- Recent studies have shown that various synthetic as well as therapeutically active naturally occurring flavonols possess novel luminescence properties that can potentially serve as highly sensitive monitors of their microenvironments in biologically relevant systems. We report a study on the interactions of bovine serum albumin (BSA) with the model flavonol 3-hydroxyflavone (3HF), using the excited-state proton-transfer (ESPT) luminescence of 3HF as a probe. Upon addition of BSA to the flavonoid solutions, we observe remarkable changes in the absorption, ESPT fluorescence emission and excitation profiles as well as anisotropy (r) values. Complexation of 3HF with protein results in a pronounced shift (20 nm) of the ESPT emission maximum of the probe (from lambda(max)(em) = 513 nm to lambda(max)(em) = 533 nm) accompanied by a significant increase in fluorescence intensity. The spectral data also suggest that, in addition to ESPT, the protein environment induces proton abstraction from 3HF leading to formation of anionic species in the ground state. Fairly high values of anisotropy are observed in the presence of BSA for the tautomer (r = 0.25) as well as anion (r = 0.35) species of 3HF, implying that both the species are located in motion-restricted environments of BSA molecules. 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 of 1.1 - 1.3 x 10(5) M(-1) for both these sites. Proteins 2001;43:75-81.
- Subjects :
- Flavonoids
Binding Sites
biology
3-Hydroxyflavone
Serum Albumin, Bovine
Models, Theoretical
Photochemistry
Biochemistry
Fluorescence
Binding constant
Tautomer
chemistry.chemical_compound
Spectrometry, Fluorescence
chemistry
Energy Transfer
Structural Biology
biology.protein
Molecule
Anisotropy
Bovine serum albumin
Absorption (chemistry)
Protons
Luminescence
Molecular Biology
Fluorescent Dyes
Subjects
Details
- ISSN :
- 08873585
- Volume :
- 43
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- Proteins
- Accession number :
- edsair.doi.dedup.....54414f424b254a9d6d470cdc61b59ab7