Search results for: PROTEIN MISFOLDING

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

  Publication

  • J. Wawer
  • J. Krakowiak
  • M. Szociński
  • Z. Lustig
  • M. Olszewski
  • K. Szostak

  - INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES - Year 2014

  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...

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• Hydration of Simple Model Peptides in Aqueous Osmolyte Solutions

  Publication

  • A. Panuszko
  • M. Pieloszczyk
  • A. Kuffel
  • K. Jacek
  • K. Biernacki
  • S. Demkowicz
  • J. Stangret
  • P. Bruździak

  - INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES - Year 2021

  The biology and chemistry of proteins and peptides are inextricably linked with water as the solvent. The reason for the high stability of some proteins or uncontrolled aggregation of others may be hidden in the properties of their hydration water. In this study, we investigated the effect of stabilizing osmolyte–TMAO (trimethylamine N-oxide) and destabilizing osmolyte–urea on hydration shells of two short peptides, NAGMA (N-acetyl-glycine-methylamide)...

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