Neurotoxicity of prion peptides mimicking the central domain of the cellular prion protein

The physiological functions of PrP(C) remain enigmatic, but the central domain, comprising highly conserved regions of the protein may play an important role. Indeed, a large number of studies indicate that synthetic peptides containing residues 106-126 (CR) located in the central domain (CD, 95-133...

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Detalles Bibliográficos
Autores: Vilches Saez, Silvia, Vergara Paños, Cristina, Nicolás i Pallejà, Josep Oriol, Sanclimens Pérez de Rozas, Glòria, Varón, S., Acosta, Gerardo A., Albericio Palomera, Fernando, Royo Expósito, Miriam, Río Fernández, José Antonio del, Gavín Marín, Rosalina
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2013
País:España
Institución:Universidad de Barcelona
Repositorio:Dipòsit Digital de la UB
OAI Identifier:oai:diposit.ub.edu:2445/46331
Acceso en línea:https://hdl.handle.net/2445/46331
Access Level:acceso abierto
Palabra clave:Prions
Pèptids
Proteïnes
Síntesi de pèptids
Mort cel·lular
Peptides
Proteins
Peptide synthesis
Cell death
Descripción
Sumario:The physiological functions of PrP(C) remain enigmatic, but the central domain, comprising highly conserved regions of the protein may play an important role. Indeed, a large number of studies indicate that synthetic peptides containing residues 106-126 (CR) located in the central domain (CD, 95-133) of PrP(C) are neurotoxic. The central domain comprises two chemically distinct subdomains, the charge cluster (CC, 95-110) and a hydrophobic region (HR, 112-133). The aim of the present study was to establish the individual cytotoxicity of CC, HR and CD. Our results show that only the CD peptide is neurotoxic. Biochemical, Transmission Electron Microscopy and Atomic Force Microscopy experiments demonstrated that the CD peptide is able to activate caspase-3 and disrupt the cell membrane, leading to cell death.

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