Abstract
The cytotoxicity of hPrP[173-195] prion peptide against a neuroblastoma cell model was found independent of its tendency to aggregate over time. Cytosolic and nuclear inclusions of peptide were highlighted by confocal microscopy, suggesting a role as a transcription factor in activating signal transduction pathways involved in cell toxicity.
Keywords: Prion disease, cellular prion protein (PrPC), helix-2, structural ambivalence, synthetic prion peptides, confocal microscopy