Interaction of Prussian blue nanoparticles with bovine serum albumin: a multi-spectroscopic approach
| Autor: | Hongyu Zhou, Fangang Meng, Wei Gu, Ling Ye, Xin Shi, Yuanjie Fan, Zhiying He |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
030103 biophysics Conformational change Analytical chemistry Nanoparticle 02 engineering and technology Intrinsic fluorescence Photochemistry 03 medical and health sciences chemistry.chemical_compound X-Ray Diffraction Structural Biology Animals Particle Size Bovine serum albumin Molecular Biology Synchronous fluorescence Prussian blue Binding Sites biology Circular Dichroism Model protein Serum Albumin Bovine General Medicine 021001 nanoscience & nanotechnology Circular dichroism spectra Spectrometry Fluorescence chemistry biology.protein Nanoparticles Thermodynamics Cattle Spectrophotometry Ultraviolet 0210 nano-technology Algorithms Ferrocyanides Protein Binding |
| Zdroj: | Journal of Biomolecular Structure and Dynamics. 36:254-261 |
| ISSN: | 1538-0254 0739-1102 |
| DOI: | 10.1080/07391102.2016.1274273 |
| Popis: | Owning to their exceptional properties, Prussian blue nanoparticles (PBNPs) are promising in a variety of biomedical applications. In this scenario, understanding of how PBNPs interact and behave in biological systems is essential. Herein, the interaction of PBNPs with protein was investigated. Specifically, the citric acid stabilized PBNPs with a size of 10 nm were synthesized and characterized. The interactions of these PBNPs with the model protein, bovine serum albumin (BSA), were then probed by spectroscopic methods. It was found that the BSA intrinsic fluorescence was quenched upon addition of PBNPs due to the static interaction, suggesting the binding of PBNPs with BSA. Moreover, the synchronous fluorescence and circular dichroism spectra indicated the conformational change of BSA due to the presence of PBNPs. |
| Databáze: | OpenAIRE |
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