Journal of Proteomics & Bioinformatics
Open Access
ISSN: 0974-276X
ISSN: 0974-276X
Salvador Ventura
Universitat Aut�?²noma de Barcelona, Spain
Posters-Accepted Abstracts: J Proteomics Bioinform
Typical amyloid diseases such as Alzheimer��?Vs and Parkinson��?s were thought to exclusively result from de novo aggregation but recently it was shown that amyloids formed in one cell can cross-seed aggregation in other cells or even individuals following a prion-like mechanism. Despite the large experimental effort devoted to understanding the phenomenon of prion transmissibility, it is still poorly understood how this property is encoded in the primary sequence. In many cases, prion structural conversion is driven by the presence of relatively large glutamine/asparagine (Q/N) enriched segments. Several studies suggest that it is the amino acid composition of these regions rather than their specific sequence that accounts for their priogenicity. However, our analysis indicates that it is instead the presence and potency of specific short amyloid-prone sequences that occur within intrinsically disordered Q/Nrich regions that determine their prion behavior modulated by the structural and compositional context. This provides a basis for the accurate identification and evaluation of prion candidate sequences in proteomes in the context of a unified framework for amyloid formation and prion propagation.
Email: 1003624@uab.cat