title: Inhibition of amyloid fibril formation of hen egg white lysozyme by trimethylamine N-oxide at low pH.
abstract: In vitro inhibition of the formation of fibrous aggregates of proteins (amyloids) has gained increasing attention due to the number of diseases associated with protein misfolding and fibrillation. An interesting group of compounds for which pronounced activity against this phenomenon can be expected consists of low molecular weight substances (osmolytes) which have the ability to change protein stability. Here we investigate the influence of trimethylamine N-oxide (TMAO) in acidic solution (pH=2) on the fibrillation of hen egg white lysozyme (HEWL). The process was monitored by five techniques: circular dichroism in the UV region, atomic force microscopy, dynamic light scattering, densimetry and gel electrophoresis. The obtained results show that protonated TMAO in a concentration of 400 mM inhibits amyloidogenesis. In the conditions of the experiment the HEWL molecules form clusters about 30 nm in diameter containing a relatively high fraction of covalent-bonded dimers.
authors.affiliation: Department of Physical Chemistry, Faculty of Chemistry, Gdańsk University of Technology, Narutowicza Str. 11/12, 80-233 Gdańsk, Poland. Electronic address: jarwawer@pg.gda.pl.
authors.forename: Jarosław
authors.initials: J
authors.lastname: Wawer
authors.affiliation: Department of Physical Chemistry, Faculty of Chemistry, Gdańsk University of Technology, Narutowicza Str. 11/12, 80-233 Gdańsk, Poland.
authors.forename: Joanna
authors.initials: J
authors.lastname: Krakowiak
authors.affiliation: Department of Electrochemistry, Corrosion and Materials Engineering, Faculty of Chemistry, Gdańsk University of Technology, Narutowicza Str. 11/12, 80-233 Gdańsk, Poland.
authors.forename: Michał
authors.initials: M
authors.lastname: Szociński
authors.affiliation: Department of Chemical Technology, Faculty of Chemistry, Gdańsk University of Technology, Narutowicza Str. 11/12, 80-233 Gdańsk, Poland.
authors.forename: Zofia
authors.initials: Z
authors.lastname: Lustig
authors.affiliation: Department of Microbiology, Faculty of Chemistry, Gdańsk University of Technology, Narutowicza Str. 11/12, 80-233 Gdańsk, Poland.
authors.forename: Marcin
authors.initials: M
authors.lastname: Olszewski
authors.affiliation: Department of Physical Chemistry, Faculty of Chemistry, Gdańsk University of Technology, Narutowicza Str. 11/12, 80-233 Gdańsk, Poland.
authors.forename: Kamila
authors.initials: K
authors.lastname: Szostak
mesh_terms: D000682:Amyloid / Q000737:chemistry* / Q000648:ultrastructure; D000818:Animals; D004529:Egg White / Q000737:chemistry*; D005260:Female; D006863:Hydrogen-Ion Concentration; D008744:Methylamines / Q000737:chemistry*; D009113:Muramidase / Q000737:chemistry*
chemical_list: D000682:Amyloid; D008744:Methylamines; C421864:hen egg lysozyme; D009113:Muramidase; C005855:trimethyloxamine
keywords: Amyloid inhibition; Hen egg white lysozyme; Protein aggregation; Protein dimerisation; Trimethylamine N-oxide