Prions are the etiological agent of fatal neurodegenerative diseases called prion diseases or transmissible spongiform encephalopathies. These maladies can be sporadic, genetic or infectious disorders. Prions are due to post-translational modifications of the cellular prion protein leading to the formation of a β-sheet enriched conformer with altered biochemical properties. The molecular events causing prion formation in sporadic prion diseases are still elusive. Recently, we published a research elucidating the contribution of major structural determinants and environmental factors in prion protein folding and stability. Our study highlighted the crucial role of octarepeats in stabilizing prion protein; the presence of a highly enthalpically stable intermediate state in prion-susceptible species; and the role of disulfide bridge in preserving native fold thus avoiding the misfolding to a β-sheet enriched isoform. Taking advantage from these findings, in this work we present new insights into structural determinants of prion protein folding and stability.
|Titolo:||New insights into structural determinants of prion protein folding and stability|
|Autori:||Benetti, F.; Legname, G.|
|Data di pubblicazione:||2015|
|Digital Object Identifier (DOI):||10.1080/19336896.2015.1022023|
|Fulltext via DOI:||10.1080/19336896.2015.1022023|
|Appare nelle tipologie:||1.1 Journal article|