Inhibition of amyloid fibril formation of hen egg white lysozyme by trimethylamine N-oxide at low pH

Jarosław Wawer; Joanna Krakowiak; Michał Szociński; Zofia Lustig; Marcin Olszewski; Kamila Szostak

doi:10.1016/j.ijbiomac.2014.06.057

Inhibition of amyloid fibril formation of hen egg white lysozyme by trimethylamine N-oxide at low pH

Int J Biol Macromol. 2014 Sep:70:214-21. doi: 10.1016/j.ijbiomac.2014.06.057. Epub 2014 Jul 7.

Authors

Jarosław Wawer¹, Joanna Krakowiak², Michał Szociński³, Zofia Lustig⁴, Marcin Olszewski⁵, Kamila Szostak²

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.gda.pl.
² Department of Physical Chemistry, Faculty of Chemistry, Gdańsk University of Technology, Narutowicza Str. 11/12, 80-233 Gdańsk, Poland.
³ Department of Electrochemistry, Corrosion and Materials Engineering, Faculty of Chemistry, Gdańsk University of Technology, Narutowicza Str. 11/12, 80-233 Gdańsk, Poland.
⁴ Department of Chemical Technology, Faculty of Chemistry, Gdańsk University of Technology, Narutowicza Str. 11/12, 80-233 Gdańsk, Poland.
⁵ Department of Microbiology, Faculty of Chemistry, Gdańsk University of Technology, Narutowicza Str. 11/12, 80-233 Gdańsk, Poland.

PMID: 25010474
DOI: 10.1016/j.ijbiomac.2014.06.057

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.

Keywords: Amyloid inhibition; Hen egg white lysozyme; Protein aggregation; Protein dimerisation; Trimethylamine N-oxide.

Publication types

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

MeSH terms

Amyloid / chemistry*
Amyloid / ultrastructure
Animals
Egg White / chemistry*
Female
Hydrogen-Ion Concentration
Methylamines / chemistry*
Muramidase / chemistry*

Substances

Amyloid
Methylamines
hen egg lysozyme
Muramidase
trimethyloxamine