Fluorescence quenching study on the interaction of ferroferric oxide nanoparticles with bovine serum albumin
| Autor: | Runguang Sun, Ying Feng, Xu Guangkuan, Changchun Hao, Linhao Lu, Wenyuan Sun |
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| Rok vydání: | 2016 |
| Předmět: |
Protein Conformation
Analytical chemistry Nanoparticle 02 engineering and technology 010402 general chemistry Photochemistry 01 natural sciences Analytical Chemistry Hydrophobic effect symbols.namesake mental disorders Animals Bovine serum albumin Magnetite Nanoparticles Instrumentation health care economics and organizations Spectroscopy Quenching (fluorescence) biology Hydrogen bond Chemistry Intermolecular force technology industry and agriculture Serum Albumin Bovine 021001 nanoscience & nanotechnology Binding constant Atomic and Molecular Physics and Optics 0104 chemical sciences Spectrometry Fluorescence biology.protein symbols Thermodynamics Cattle van der Waals force 0210 nano-technology Protein Binding |
| Zdroj: | Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy. 184 |
| ISSN: | 1873-3557 |
| Popis: | Fluorescence quenching was used to study the potential interaction mechanism of Bovine serum albumin (BSA) with either hydrophilic ferroferric oxide (Fe3O4) nanoparticles (NPs) or hydrophobic Fe3O4 NPs. The experimental results indicated the mechanism between BSA and hydrophilic Fe3O4 NPs was static quenching and the one between BSA and hydrophobic Fe3O4 NPs was dynamic process that was drove by Forster's resonance energy transfer (FRET). And the binding parameters for the interaction of BSA with either hydrophilic or hydrophobic Fe3O4 NPs were calculated by using the fluorescence quenching measurement. The binding constant (KA) values of hydrophilic Fe3O4 NPs were 8518.73 ± 23.35 (at 298 K), 1190.31 ± 15.41 (at 306 K) and 321.97 ± 8.57 (at 313 K), respectively. The thermodynamic analysis implied that the intermolecular forces between BSA and hydrophilic Fe3O4 NPs were Van der Waals interaction or hydrogen bond, because the values of ΔH and ΔS between them were negative. While the one of BSA and hydrophobic Fe3O4 NPs involved hydrophobic forces, owing to the positive ΔH and ΔS between them. But they were all enthalpy-driven and exothermic, since their ΔG values were all negative. Synchronous fluorescence spectroscopy suggested that the conformation of tryptophan residue of BSA was changed in the presence of hydrophilic Fe3O4 NPs or hydrophobic Fe3O4 NPs, because the position of the maximum emission wavelength had a discernible red shift. |
| Databáze: | OpenAIRE |
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