Pressure-induced amorphization in biopolymers

K. Heremans, Carolien Dirix, Filip Meersman, Helge Pfeiffer, Laszlo Smeller

Research output: Contribution to journalArticle

5 Citations (Scopus)


Pressure-induced unfolding of proteins in solution shows analogies to the pressure-induced amorphization observed in some inorganic and polymer systems. More specifically, pressure gives rise to conformations that show a strong tendency to form supramolecular aggregates that have some relevance to molecular diseases. Hydrostatic pressure can tune the conformation of 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)11477-11484
Number of pages8
JournalJournal of Physics Condensed Matter
Issue number44 SPEC ISS.
Publication statusPublished - Nov 11 2002


ASJC Scopus subject areas

  • Materials Science(all)
  • Condensed Matter Physics

Cite this

Heremans, K., Dirix, C., Meersman, F., Pfeiffer, H., & Smeller, L. (2002). Pressure-induced amorphization in biopolymers. Journal of Physics Condensed Matter, 14(44 SPEC ISS.), 11477-11484.