Protein thermal stabilization in aqueous solutions of osmolytes.

Piotr Bruździak; Aneta Panuszko; Muriel Jourdan; Janusz Stangret

doi:10.18388/abp.2014_950

Protein thermal stabilization in aqueous solutions of osmolytes.

Piotr Bruździak Department of Physical Chemistry, Chemical Faculty, Gdansk University of Technology, Gdańsk, Poland.;
Aneta Panuszko Department of Physical Chemistry, Chemical Faculty, Gdansk University of Technology, Gdańsk, Poland.;
Muriel Jourdan Département de Chimie Moléculaire, CNRS UMR5250, ICMG FR2607, Université de Grenoble, 570 Grenoble Cedex 9, France.;
Janusz Stangret Department of Physical Chemistry, Chemical Faculty, Gdansk University of Technology, Gdańsk, Poland.;

DOI: https://doi.org/10.18388/abp.2014_950

Abstract

Proteins' thermal stabilization is a significant problem in various biomedical, biotechnological, and technological applications. We investigated thermal stability of hen egg white lysozyme in aqueous solutions of the following stabilizing osmolytes: Glycine (GLY), N-methylglycine (NMG), N,N-dimethylglycine (DMG), N,N,N-trimethylglycine (TMG), and trimethyl-N-oxide (TMAO). Results of CD-UV spectroscopic investigation were compared with FTIR hydration studies' results. Selected osmolytes increased lysozyme's thermal stability in the following order: Gly>NMG>TMAO≈DMG>TMG. Theoretical calculations (DFT) showed clearly that osmolytes' amino group protons and water molecules interacting with them played a distinctive role in protein thermal stabilization. The results brought us a step closer to the exact mechanism of protein stabilization by osmolytes.

Published

2015-10-23

Issue

Vol. 63 No. 1 (2016)

Section

Articles

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