Interaction of quercetin with ovalbumin: Spectroscopic and molecular modeling studies
| Autor: | Gong-Ke Wang, Sheng-Hua Gao, Yan Lu, Dejun Chen, Changling Yan, Yun-Lai Wang |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
musculoskeletal diseases
Molecular model biology Hydrogen bond Stereochemistry Chemistry Biophysics Active site General Chemistry Condensed Matter Physics Biochemistry Acceptor Atomic and Molecular Physics and Optics Fluorescence spectroscopy Accessible surface area body regions Hydrophobic effect Förster resonance energy transfer Computational chemistry biology.protein |
| Zdroj: | Journal of Luminescence. 129:1048-1054 |
| ISSN: | 0022-2313 |
| Popis: | The binding of quercetin (QCT) to ovalbumin (OVA) in aqueous solution was investigated by molecular spectroscopy and modeling at pH 7.4. The fluorescence, synchronous fluorescence and UV-absorption spectroscopies were employed to study the mode and the mechanism for this interaction. QCT binding is characterized by one high affinity binding site with the association constants of the order of 10 5 . The distance between donor (OVA) and acceptor (QCT) was estimated according to Forster's theory of non-radiation energy transfer. Molecular docking showed that the QCT can bind to the active site of OVA. The binding dynamics was expounded by thermodynamic parameters, molecular modeling and accessible surface area calculation, which entails that hydrophobic interactions, hydrogen bonding and electrostatic forces stabilizes the interaction. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect