Amyloid fibril formation in the presence of water structure-affecting solutes

Jarosław Wawer; Emilia Kaczkowska; Jakub Karczewski; Marcin Olszewski; Danuta Augustin-Nowacka; Joanna Krakowiak

doi:10.1016/j.bpc.2019.106265

Amyloid fibril formation in the presence of water structure-affecting solutes

Biophys Chem. 2019 Nov:254:106265. doi: 10.1016/j.bpc.2019.106265. Epub 2019 Sep 12.

Authors

Jarosław Wawer¹, Emilia Kaczkowska², Jakub Karczewski³, Marcin Olszewski⁴, Danuta Augustin-Nowacka⁵, Joanna Krakowiak²

Affiliations

¹ Department of Physical Chemistry, Faculty of Chemistry, Gdańsk University of Technology, Narutowicza Str. 11/12, 80-233 Gdańsk, Poland. Electronic address: jarwawer@pg.edu.pl.
² Department of Physical Chemistry, Faculty of Chemistry, Gdańsk University of Technology, Narutowicza Str. 11/12, 80-233 Gdańsk, Poland.
³ Department of Solid State Physics, Faculty of Applied Physics and Mathematics, Gdańsk University of Technology, Narutowicza Str. 11/12, 80-233 Gdańsk, Poland.
⁴ Department of Molecular Biotechnology and Microbiology, Faculty of Chemistry, Gdańsk University of Technology, Narutowicza Str. 11/12, 80-233 Gdańsk, Poland.
⁵ Faculty of Chemistry, University of Gdańsk, Wita Stwosza Str. 63, 80-308 Gdańsk, Poland.

PMID: 31669866
DOI: 10.1016/j.bpc.2019.106265

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 (250mM BU and 500mM 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.

Keywords: Amyloid; Hen egg white lysozyme; Hydrophobic hydration; Protein aggregation; Water structure breakers.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amyloid / chemistry*
Animals
Chickens
Circular Dichroism
Microscopy, Atomic Force
Muramidase / chemistry*
Muramidase / metabolism
Protein Stability
Solutions / chemistry
Urea / chemistry
Water / chemistry*

Substances

Amyloid
Solutions
Water
Urea
hen egg lysozyme
Muramidase