Journal article
Neutron reflectometry studies define prion protein N-terminal peptide membrane binding
AP Le Brun, CL Haigh, SC Drew, M James, MP Boland, SJ Collins
Biophysical Journal | CELL PRESS | Published : 2014
Abstract
The prion protein (PrP), widely recognized to misfold into the causative agent of the transmissible spongiform encephalopathies, has previously been shown to bind to lipid membranes with binding influenced by both membrane composition and pH. Aside from the misfolding events associated with prion pathogenesis, PrP can undergo various posttranslational modifications, including internal cleavage events. Alpha- and beta-cleavage of PrP produces two N-terminal fragments, N1 and N2, respectively, which interact specifically with negatively charged phospholipids at low pH. Our previous work probing N1 and N2 interactions with supported bilayers raised the possibility that the peptides could insert..
View full abstractRelated Projects (3)
Grants
Awarded by Australian Nuclear Science and Technology Organisation
Funding Acknowledgements
This work was supported by the Australian Nuclear Science and Technology Organisation (ANSTO), proposal ID2211, Australian Institute for Nuclear Science and Engineering (AINSE Ltd.) for travel support, and a National Health and Medical Research Council (NHMRC) program grant (No. 628946). S. J. C. is funded by an NHMRC Practitioner Fellowship (No. APP100581). S. C. D. is funded by an Australian Research Council Future Fellowship (FT110100199). A. P. L. B. is funded by an Australian Research Council Discovery Early Career Research Award (DE140101788). The authors declare that they have no conflicts of interest.