Contact-induced structure transformation in transmembrane prion propagation

D. M. Ou, C. C. Chen*, C. M. Chen

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)


Based on recent experimental evidences of the transmission of prion diseases due to a particular transmembrane form (termed CtmPrP), we propose a theoretical model for the molecular mechanism of such conformational diseases, in which a misfolded CtmPrP induces a similar misfolding of another CtmPrP. Computer simulations are performed to investigate the correlation between folding time and the concentration of misfolded PrP in various processes, including dimerization, trimerization, and cooperative dimerization. By comparing with the experimental correlation curve between incubation time and injected dose of scrapie prions, we conclude that cooperative dimerization may play an important role in the pathological mechanism of prion diseases.

Original languageEnglish
Pages (from-to)2704-2710
Number of pages7
JournalBiophysical Journal
Issue number8
Publication statusPublished - 2007 Apr

ASJC Scopus subject areas

  • Biophysics


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