Intermolecular interactions of proteins under pressure. Aggregation, dissociation, chaperoning

László Smeller, Filip Meersman, Judit Fidy, Karel Heremans

Research output: Contribution to journalConference article

1 Citation (Scopus)


The effect of pressure on the aggregation ability of proteins is summarized in this paper. It is shown that pressure counteracts the formation of intermolecular β-structure, which is the main structural form in conformational diseases. Already slight pressurization to typically 2 kbar can destabilize aggregates. On the other hand, the intermediate state formed after high pressure treatment, has increased tendency for aggregation. It is shown that pressure is an appropriate tool for the studying the formation and the stability of aggregates.

Original languageEnglish
Pages (from-to)19-24
Number of pages6
JournalDefect and Diffusion Forum
Publication statusPublished - Jan 1 2002
Event4th High Pressure School on Chemistry, Biology, Materials Science and Techniques - Warswaw, Poland
Duration: Jun 22 2001Jun 25 2001


  • Aggregation
  • Amyloid
  • Chaperone
  • Dissociation
  • FTIR
  • Fibrillogenesis
  • High Pressures
  • Myoglobin
  • Protein

ASJC Scopus subject areas

  • Radiation
  • Materials Science(all)
  • Condensed Matter Physics

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