Contact-induced structure transformation in transmembrane prion propagation

D. M. Ou; C. C. Chen; C. M. Chen

doi:10.1529/biophysj.106.098335

Contact-induced structure transformation in transmembrane prion propagation

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

^*Corresponding author for this work

Department of Physics

Research output: Contribution to journal › Article › peer-review

4 Citations (Scopus)

Abstract

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 language	English
Pages (from-to)	2704-2710
Number of pages	7
Journal	Biophysical Journal
Volume	92
Issue number	8
DOIs	https://doi.org/10.1529/biophysj.106.098335
Publication status	Published - 2007 Apr

ASJC Scopus subject areas

Biophysics

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title = "Contact-induced structure transformation in transmembrane prion propagation",

abstract = "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.",

author = "Ou, {D. M.} and Chen, {C. C.} and Chen, {C. M.}",

note = "Funding Information: We acknowledge partial support by the National Science Council of Taiwan under grant No. NSC 94-2112-M-003-012. ",

year = "2007",

month = apr,

doi = "10.1529/biophysj.106.098335",

language = "English",

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journal = "Biophysical Journal",

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T1 - Contact-induced structure transformation in transmembrane prion propagation

AU - Ou, D. M.

AU - Chen, C. C.

AU - Chen, C. M.

N1 - Funding Information: We acknowledge partial support by the National Science Council of Taiwan under grant No. NSC 94-2112-M-003-012.

PY - 2007/4

Y1 - 2007/4

N2 - 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.

AB - 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.

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DO - 10.1529/biophysj.106.098335

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VL - 92

SP - 2704

EP - 2710

JO - Biophysical Journal

JF - Biophysical Journal

IS - 8

ER -

Contact-induced structure transformation in transmembrane prion propagation

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