Biochemical evaluation of a synthesized isoflavone-selenium complex by molecular spectra
| Autor: | Hua-xin Zhang, Zhen-xia Huang |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
Circular dichroism
Ibuprofen symbols.namesake Albumins Organoselenium Compounds Genetics Molecule Animals Bovine serum albumin Selenium Compounds Molecular Biology Binding Sites biology Chemistry Hydrogen bond Serum Albumin Bovine General Medicine Fluorescence Isoflavones Intramolecular force biology.protein symbols Physical chemistry Thermodynamics Fluorescence cross-correlation spectroscopy Cattle Warfarin van der Waals force Protein Binding |
| Zdroj: | Molecular biology reports. 39(7) |
| ISSN: | 1573-4978 |
| Popis: | A coordination compound of 5, 7-dihydrox-4'-methoxyisoflavone and selenium was synthesized and its structure was identified by IR, LC-MS and (1)H-NMR. Its biochemical effects were investigated using bovine serum albumin (BSA) as a target protein molecule, in which process three-dimensional (3D) fluorescence spectra, ultraviolet spectra, circular dichroism (CD) spectra and fluorescence probe techniques were employed. The interaction of SEIF and BSA was discussed by fluorescence quenching method and Forster non-radiation energy transfer theory. The thermodynamic parameters ΔH (θ), ΔG (θ), ΔS (θ) at different temperatures were calculated according to Van't Hoff isobaric equation and the results indicated the interaction was an exothermic as well as a spontaneous process. The binding site was explored by fluorescence probe method using warfarin and ibuprofen as markers. Intramolecular forces which are responsible for maintaining the binding were mainly hydrogen bond and van der Waals power. The average distance from the tryptophan residue in domain II of BSA (donor) to SEIF (acceptor) is 3.57 nm at body temperature. The conformation changes of BSA were investigated by 3D fluorescence and CD spectra. |
| Databáze: | OpenAIRE |
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