Jump to main content
Jump to site search
Access to RSC content Close the message box

Continue to access RSC content when you are not at your institution. Follow our step-by-step guide.


Issue 6, 2007
Previous Article Next Article

Steered molecular dynamics studies reveal different unfolding pathways of prions from mammalian and non-mammalian species

Author affiliations

Abstract

Prion diseases are associated with an abnormal conformational transition involving the prion protein and are known to affect mammals. Here, the different mechanical behaviour of two mammalian, human (HuPrP) and Syrian hamster (ShaPrP), and two non-mammalian, chicken (ChPrP) and turtle (TuPrP), prions was assessed by steered molecular dynamics simulations performed on the globular domains of the four proteins. In mammalian prions a greater resistance to external stretching forces and an earlier occurrence of irreversible events were observed. The different unfolding profile of mammalian prions, ascribable to the intramolecular interactions involving helix 1 with helix 3, implicate the existence of metastable non-native states which may prompt abnormal pathways of protein misfolding and aggregation.

Graphical abstract: Steered molecular dynamics studies reveal different unfolding pathways of prions from mammalian and non-mammalian species

Back to tab navigation

Article information


Submitted
17 Jan 2007
Accepted
08 Mar 2007
First published
28 Mar 2007

New J. Chem., 2007,31, 901-905
Article type
Paper

Steered molecular dynamics studies reveal different unfolding pathways of prions from mammalian and non-mammalian species

M. Pappalardo, D. Milardi, D. Grasso and C. La Rosa, New J. Chem., 2007, 31, 901
DOI: 10.1039/B700764G

Social activity

Search articles by author

Spotlight

Advertisements