Bovine serum albumin adsorption on SiO2 and TiO2 nanoparticle surfaces at circumneutral and acidic pH: A tale of two nano-bio surface interactions
| Autor: | Zhenzhu Xu, Brittany E. Givens, Vicki H. Grassian, Jennifer Fiegel |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
Thermogravimetric analysis
biology Chemistry Nanoparticle Protein Corona 02 engineering and technology 010402 general chemistry 021001 nanoscience & nanotechnology 01 natural sciences 0104 chemical sciences Surfaces Coatings and Films Electronic Optical and Magnetic Materials Biomaterials Colloid and Surface Chemistry Adsorption Attenuated total reflection biology.protein Organic chemistry Fourier transform infrared spectroscopy Bovine serum albumin 0210 nano-technology Protein adsorption Nuclear chemistry |
| Zdroj: | Journal of Colloid and Interface Science. 493:334-341 |
| ISSN: | 0021-9797 |
| Popis: | The interaction of a model protein, bovine serum albumin (BSA) with two different metal oxide nanoparticles, TiO2 (∼22 nm) and SiO2 (∼14 nm), was studied at both physiological and acidic pH. The pH- and nanoparticle-dependent differences in protein structure and protein adsorption were determined using attenuated total reflectance Fourier transform infrared spectroscopy (ATR-FTIR) and thermogravimetric analysis (TGA). The results indicated that the surface coverage of BSA decreases with decreasing pH on both TiO2 and SiO2 surfaces, and BSA coverage is higher by a factor of ca. 3–10 times more on TiO2 compared to SiO2. The secondary structure of BSA changes upon adsorption to either nanoparticle surface at both pH 7.4 and 2. At acidic pH, BSA appears to completely unfold on TiO2 nanoparticles whereas it assumes an extended conformation on SiO2. These differences highlight for the first time the extent to which the protein corona structure is significantly impacted by protein-nanoparticle interactions which depend on the interplay between pH and specific nanoparticle surface chemistry. |
| Databáze: | OpenAIRE |
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