Protein thermal stabilization in aqueous solutions of osmolytes

• Authors: Piotr Bruździak , Aneta Panuszko , Muriel Jourdan , Janusz Stangret
• Languages of publication: EN

Abstracts

EN

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.

Keywords

EN

water structure; protein stability; circular dichroism; FT-IR spectroscopy; DFT calculations

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2016
• Volume: 63
• Issue: 1
• Pages: 65-70

Dates

published

2016

received

2014-12-03

revised

2015-06-19

accepted

2015-09-22

(unknown)

2015-10-23

Contributors

author

Piotr Bruździak

• Department of Physical Chemistry, Chemical Faculty, Gdansk University of Technology, Gdańsk, Poland

author

Aneta Panuszko

• Department of Physical Chemistry, Chemical Faculty, Gdansk University of Technology, Gdańsk, Poland

author

Muriel Jourdan

• Département de Chimie Moléculaire, CNRS UMR5250, ICMG FR2607, Université de Grenoble, 570 Grenoble Cedex 9, France

author

Janusz Stangret

• Department of Physical Chemistry, Chemical Faculty, Gdansk University of Technology, Gdańsk, Poland

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Identifiers

DOI

10.18388/abp.2014_950