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Abstract
The impact of the differently hydrated non-electrolytes (protein structure destabilizers) on the fibrillation of hen egg white lysozyme (HEWL) was investigated. Two isomeric urea derivatives i.e. butylurea (BU) and N,N,N′,N′-tetramethylurea (TMU) were chosen as a tested compounds. The obtained results show that butylurea exerts greater impact on HEWL and its fibrillation than tetramethylurea. Both substances decrease the time of induction of the fibrillation (lag time) but only BU increases the efficiency of amyloidogenesis. For the systems with equivalent reduction of the HEWL stability (250 mM BU and 500 mM TMU) the not-equivalent increase of the protein fibrillation was recorded (higher for BU). This fact suggests that specific interactions with protein, possibly water mediated, are responsible for the action of the tested substances.
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Authors (6)
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Danuta Augustin-Nowacka
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- Category:
- Articles
- Type:
- artykuły w czasopismach
- Published in:
-
BIOPHYSICAL CHEMISTRY
no. 254,
ISSN: 0301-4622 - Language:
- English
- Publication year:
- 2019
- Bibliographic description:
- Wawer J., Kaczkowska E., Karczewski J., Olszewski M., Augustin-Nowacka D., Krakowiak J.: Amyloid fibril formation in the presence of water structure-affecting solutes// BIOPHYSICAL CHEMISTRY -Vol. 254, (2019), s.106265-
- DOI:
- Digital Object Identifier (open in new tab) 10.1016/j.bpc.2019.106265
- Verified by:
- Gdańsk University of Technology
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