From aggregation to chaperoning: Pressure effect on intermolecular interactions of proteins

L. Smeller, Filip Meersman, F. Tölgyesi, Csaba Böde, J. Fidy, Karel Heremans

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)751-756
Number of pages6
JournalHigh Pressure Research
Volume22
Issue number3-4
DOIs
Publication statusPublished - Jun 2002

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pressure effects
proteins
interactions
oligomers

Keywords

  • Aggregation
  • Amyloid
  • Chaperone
  • Dissociation
  • Filbrillogenesis
  • FTIR
  • High pressure
  • Protein

ASJC Scopus subject areas

  • Physics and Astronomy(all)

Cite this

From aggregation to chaperoning : Pressure effect on intermolecular interactions of proteins. / Smeller, L.; Meersman, Filip; Tölgyesi, F.; Böde, Csaba; Fidy, J.; Heremans, Karel.

In: High Pressure Research, Vol. 22, No. 3-4, 06.2002, p. 751-756.

Research output: Contribution to journalArticle

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