| Autor: |
Boris I. Kurganov, Evgeny N. Dobrov, V. A. Drachev, Lev S. Yaguzhinsky, M. A. Nemykh, Alexander M. Arutyunyan, Yuliy V. Panyukov, E. R. Rafikova |
| Rok vydání: |
2006 |
| Předmět: |
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| Zdroj: |
The International Journal of Biochemistry & Cell Biology. 38:533-543 |
| ISSN: |
1357-2725 |
| DOI: |
10.1016/j.biocel.2005.10.014 |
| Popis: |
Ordered and amorphous protein aggregation causes numerous diseases. Tobacco mosaic virus coat protein for many decades serves as the classical model of ordered protein aggregation ("polymerization"). It was also found to be highly prone to heat-induced amorphous aggregation and the rate of this aggregation could be easily manipulated by changes in solution ionic strength and temperature. Here, we report that rapid amorphous aggregation of this protein can be induced at 25 degrees C in phosphate buffer by low micromolar (start at about 15 microM) concentrations of cationic surfactant cetyltrimethylammonium bromide. At equilibrium four surfactant molecules bound to the protein subunit. As judged by circular dichroism and fluorescence spectroscopy data, the coat protein molecules retained their native structure upon the cetyltrimethylammonium bromide induced aggregation. No aggregation was observed at the higher surfactant concentrations (above 300 microM). Micromolar concentrations of anionic surfactant sodium dodecylsulfate rapidly reversed the cetyltrimethylammonium bromide induced aggregation of the coat protein due to formation of mixed surfactant-surfactant micelles. Cetyltrimethylammonium bromide (100-300 microM) also induced the reversible intact tobacco mosaic virus virion aggregation. The possible liability to the cetyltrimethylammonium bromide induced amorphous aggregation of other ordered aggregate-producing proteins has been discussed. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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