Chemical biology news from across RSC Publishing.
Unravelling the prion mystery
03 May 2007
Tiny differences between mammalian and non-mammalian prion proteins could be responsible for transmissible spongiform encephalopathies (TSEs) such as Creutzfeld-Jacob disease, say Italian scientists. TSEs are generally accepted to be caused by prions in the brain folding into an abnormal form; this triggers other prions to refold, creating plaques and tangles.
Models imply greater force is needed to stretch mammalian prions
The group used the simulations to model the prions, to see how far they could stretch and still refold into their native state. The team found that a greater force was needed to unfold the mammalian prions. However, once unfolded, these prions refolded into the native state less efficiently than the turtle or chicken proteins, adopting metastable configurations instead.
Link to journal article
Steered molecular dynamics studies reveal different unfolding pathways of prions from mammalian and non-mammalian species
Matteo Pappalardo, Danilo Milardi, Domenico Grasso and Carmelo La Rosa, New J. Chem., 2007, 31, 901