Protein thermal stabilization in aqueous solutions of osmolytes.
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.
Department of Physical Chemistry, Chemical Faculty, Gdansk University of Technology, Gdańsk, Poland.
Piotr
P
Bruździak
Department of Physical Chemistry, Chemical Faculty, Gdansk University of Technology, Gdańsk, Poland.
Aneta
A
Panuszko
Département de Chimie Moléculaire, CNRS UMR5250, ICMG FR2607, Université de Grenoble, 570 Grenoble Cedex 9, France.
Muriel
M
Jourdan
Department of Physical Chemistry, Chemical Faculty, Gdansk University of Technology, Gdańsk, Poland.
Janusz
J
Stangret
D002942:Circular Dichroism; D004795:Enzyme Stability; D009113:Muramidase / Q000737:chemistry*; D012996:Solutions; D017550:Spectroscopy, Fourier Transform Infrared; D014867:Water / Q000737:chemistry
D012996:Solutions; D014867:Water; D009113:Muramidase