The ambivalent effect of Fe 3 O 4 nanoparticles on the urea-induced unfolding and dilution-based refolding of lysozyme
| Autor: | F. Kashanian, Ali Akbar Moosavi-Movahedi, M Vatani, A R Bagherpour, Mehran Habibi-Rezaei |
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| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
magnetite (Fe O ) nanoparticles
Circular dichroism Biomedical Engineering Nanoparticle Bioengineering 02 engineering and technology stability 010402 general chemistry 021001 nanoscience & nanotechnology 01 natural sciences 0104 chemical sciences Biomaterials chemistry.chemical_compound chemistry hen egg white lysozyme refolding by dilution structure ordering/disordering Urea Zeta potential Denaturation (biochemistry) Protein folding Lysozyme Fourier transform infrared spectroscopy 0210 nano-technology Nuclear chemistry |
| Zdroj: | Kashanian, F, Habibi-Rezaei, M, Moosavi-Movahedi, A A, Bagherpour, A R & Vatani, M 2018, ' The ambivalent effect of Fe 3 O 4 nanoparticles on the urea-induced unfolding and dilution-based refolding of lysozyme ', Biomedical Materials, vol. 13, no. 4, 045014 . https://doi.org/10.1088/1748-605x/aab8d7 |
| Popis: | Due to the numerous biological applications of magnetite (Fe3O4) nanoparticles (MNPs), it is essential to identify the influence of these nanoparticles on basic biological processes. Therefore, in this research, the effect of MNPs on the structure and activity of hen egg white lysozyme (HEWL) (EC 3.2.1.1) as a model protein was examined using tryptophan intrinsic fluorescence, UV/Vis, and circular dichroism spectroscopy. Moreover, enzyme activities were analyzed by a turbidometric approach in the presence of MNPs at concentrations providing MNPs/HEWL ratios in the range of 0.04–1.25. As-synthesized MNPS were characterized by Fourier transform infrared spectroscopy, x-ray diffraction, scanning electron microscopy, transmission electron microscopy, vibrating sample magnetometry and the zeta potential of MNPs was measured to be −29 mV. The goal of this work was investigating the ordering or disordering effect of MNPs on protein structure at ratios lower or higher than 0.918 as concentration ratio of threshold (CRT), respectively, in order to answer the question: 'How can the denaturation and refolding of a model protein (HEWL) be affected by MNPs?' As has been reported recently, the protein folding, helicity, and half-life were improved at CRT to make the protein more disordered upon interaction with MNPs. The disordering effect of urea at >CRT and even at |
| Databáze: | OpenAIRE |
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