Biophysical influence of coumarin 35 on bovine serum albumin: Spectroscopic study
| Autor: | Yavuz Onganer, Tuğba Bayraktutan |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
Protein Conformation
Kinetics 02 engineering and technology 010402 general chemistry Photochemistry 01 natural sciences Biophysical Phenomena Analytical Chemistry Coumarins Animals Bovine serum albumin Instrumentation Spectroscopy Binding Sites Quenching (fluorescence) biology Chemistry Temperature Serum Albumin Bovine Hydrogen-Ion Concentration 021001 nanoscience & nanotechnology Acceptor Fluorescence Atomic and Molecular Physics and Optics 0104 chemical sciences Spectrometry Fluorescence Förster resonance energy transfer Energy Transfer biology.protein Cattle Spectrophotometry Ultraviolet Fluorescence cross-correlation spectroscopy Absorption (chemistry) 0210 nano-technology |
| Zdroj: | Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy. 171:90-96 |
| ISSN: | 1386-1425 |
| Popis: | The binding mechanism and protein-fluorescence probe interactions between bovine serum albumin (BSA) and coumarin 35 (C35) was investigated by using UV-Vis absorption and fluorescence spectroscopies since they remain major research topics in biophysics. The spectroscopic data indicated that a fluorescence quenching process for BSA-C35 system was occurred. The fluorescence quenching processes were analyzed using Stern-Volmer method. In this regard, Stern-Volmer quenching constants (K-sv) and binding constants were calculated at different temperatures. The distance r between BSA (donor) and 05 (acceptor) was determined by exploiting fluorescence resonance energy transfer (FRET) method. Synchronous fluorescence spectra were also studied to observe information about conformational changes. Moreover, thermodynamics parameters were calculated for better understanding of interactions and conformational changes of the system. (C) 2016 Elsevier B.V. All rights reserved. |
| Databáze: | OpenAIRE |
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