| Autor: |
Rozhkov, S. P., Goryunov, A. S., Kolodey, V. A., Pron'kina, L. A., Rozhkova, N. N. |
| Zdroj: |
Biophysics; Dec2022, Vol. 67 Issue 6, p888-894, 7p |
| Abstrakt: |
Raman spectroscopy was used to analyze the positions of extrema, amplitudes, and widths of the main Raman spectral lines in the wavenumber range 3200–3600 cm–1 attributed to stretching vibrations of a network of hydrogen bonds with a change in the concentration of bovine serum albumin in the range of 0.01–10 mg/mL. The variations of these parameters for protein in the presence and absence of fatty acids were compared; the effect of shungite carbon nanoparticles on these variations was studied. It was found that the stability of the hydrogen bond system of water depended significantly nonlinearly on the protein concentration; in the protein concentration range of 0.1–0.3 mg/mL, stabilization was maximal and decreased with both an increase and decrease in concentration. Destabilization of the hydrogen bond system with an increase in protein concentration might be associated with its conformation and/or aggregation. The changes depended both on the ligand state of bovine serum albumin (the presence of fatty acids) and the influence of shungite carbon nanoparticles. In the presence of shungite carbon nanoparticles, the hydrogen bond network was maintained in a more homogeneous and loosened state over the entire range of protein concentrations, both with and without fatty acids. The data obtained indicate the important role of water in the mechanisms of interaction between protein molecules as well as between graphenes of shungite carbon nanoparticles and the protein surface in the region of their binding centers for fatty acids. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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