The effect of pressure on the protein aggregation is shown in this paper. Deposition of insoluble protein aggregates is one of the key factors in the conformational diseases. Pressure counteracts the formation of intermolecular β-structure. Already slight pressurization to typically 2-3 kbar can destabilize aggregates of apo-horseradish peroxidase. On the other hand, the chaperone proteins, which prevent aggregation of damaged proteins exist in big oligomers. We show that pressure treatment of these aggregates changes the chaperone activity.
ASJC Scopus subject areas
- Condensed Matter Physics