Pressure-temperature effects on proteins: Unfolding, aggregation and fibrillogenesis

Filip Meersman, Helge Pfeiffer, László Smeller, Karel Heremans

Research output: Contribution to journalConference article

1 Citation (Scopus)


Several pharmaceutical, medical and food processing problems require a thorough understanding of the protein aggregation mechanism and fibrillogenesis. Here we show that hydrostatic pressure can give information on the intermediates along the unfolding/aggregation pathway. Pressure can also be used to probe the stability of the aggregate, and thus the interactions that are responsible for it. In particular we demonstrate that pressure might be an interesting tool to study the fibril formation. Fourier transform infrared spectroscopy reveals the presence of fibril secondary structures other than random coil and intermolecular β-sheet.

Original languageEnglish
Pages (from-to)47-54
Number of pages8
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
  • Compressibility
  • Fibrils
  • Phase Diagram
  • Pressure Unfolding

ASJC Scopus subject areas

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

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