Confocal Microscopy Evidence of Prion Protein Fragment hPrP[173-195] Internalization in Rat B104 Neuroblastoma Cell Line
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); confocal microscopy; helix-2; structural ambivalence; synthetic prion peptides
Document Type: Research Article
Publication date: 01 November 2009
- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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