Molecular spectroscopic studies on the interaction of morin with bovine serum albumin
| Autor: | Si-Si Zhang, Xiao-Ling Li, Yan-Jun Hu, Hua-Li Yue, E. Tang, Li-Ping Zhang |
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| Rok vydání: | 2012 |
| Předmět: |
Circular dichroism
Protein Conformation Stereochemistry Metal ions in aqueous solution Biophysics Morin Antioxidants Hydrophobic effect chemistry.chemical_compound Radiology Nuclear Medicine and imaging Binding site Bovine serum albumin Flavonoids Binding Sites Radiation Quenching (fluorescence) Radiological and Ultrasound Technology biology Chemistry Circular Dichroism Temperature Serum Albumin Bovine Binding constant Crystallography Spectrometry Fluorescence Metals biology.protein Spectrophotometry Ultraviolet Protein Binding |
| Zdroj: | Journal of Photochemistry and Photobiology B: Biology. 112:16-22 |
| ISSN: | 1011-1344 |
| DOI: | 10.1016/j.jphotobiol.2012.04.001 |
| Popis: | The interaction between morin and bovine serum albumin (BSA) was studied using molecular spectroscopic approach at different temperatures under imitated physiological conditions. Quenching of intrinsic tryptophanyl fluorescence of BSA with increasing morin concentration is the actuating tool in the analysis. The obtained quenching mechanisms, binding constants, binding sites and corresponding thermodynamic parameters at different temperatures indicate that the hydrophobic interaction play a major role in the morin-BSA association. Binding affinity between morin and BSA was determined using Scatchard equation and the modified Stern-Volmer equation, and the corresponding Structure-affinity relationships of flavonoids were discussed. Site marker competitive displacement experiments demonstrated that morin binds with high affinity to site II (subdomain IIIA) of BSA. Furthermore, the circular dichroism spectral results indicated that the conformation of BSA changed in the presence of morin. In addition, the effect of some common metal ions on the binding constant between morin and BSA was examined. |
| Databáze: | OpenAIRE |
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