| Autor: |
Muranov, K. O., Poliansky, N. B., Kleimenov, S. Yu., Ostrovsky, M. A. |
| Zdroj: |
Russian Journal of Physical Chemistry B: Focus on Physics; Nov2019, Vol. 13 Issue 6, p928-931, 4p |
| Abstrakt: |
The small heat shock protein α-crystallin is a main protein in the lens of the eye. It supports lens transparency by blocking the aggregation of damaged proteins in the cytoplasm of lens fiber cells. Using detergent-induced protein denaturation, it was shown that α-crystallin supports the refolding of denatured proteins. The aim of this paper was to study the ability of α-crystallin to restore the native structure of the physiologically relevant substrate of UV-damaged βL-crystallin. It was shown α-crystallin brakes the aggregation of UV-damaged βL-crystallin at conditions close to physiological (temperature, pH, solvent ionic strength). Full blocking of aggregation was obtained at a 5/1 ratio of α-crystallin and the target protein (mol/mol). DSC study has shown that denaturation temperatures of native, UV-damaged βL-crystallin and UV-damaged βL-crystallin incubated with α-crystallin for 24 h were not different and were equally of 64.0 ± 0.3°C. The total energy of the denaturation of stable water-soluble forms of UVβL-crystallin did not differ from the denaturation energy of UVβL-crystallin incubated with α-crystallin for 24 h. These results directly indicate that the interaction of denatured UVβL-crystallin and α-crystallin does not lead to the refolding of denatured protein. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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