Prion Protein (106-126) (trifluoroacetate salt)

Prion Protein (106-126) is a peptide fragment of the cellular prion protein PrPc. It forms fibrils that are organized into β-strands, a behavior characteristic of amyloids. It is toxic to primary rat hippocampal neurons at a concentration of 80 μM following incubation for 10 days and induces DNA fragmentation and apoptosis. Prion Protein (106-126) (25 μM) activates ERK1 and 2, p38, and JNK1 and 2 kinases, induces apoptosis, increases NADPH oxidase-dependent production of reactive oxygen species (ROS), and decreases glutathione (GSH) levels in 1C115-HT serotonergic and 1C11NE noradrenergic differentiated neuronal cells. It forms channels in lipid bilayer membranes that are freely permeable to calcium, sodium, potassium, lithium, rubidium, cesium, and chloride ions at a concentration of 20 μM, and channel formation is significantly enhanced by aging and low pH. In vivo, intraocular injection of prion protein (106-126) (1 mM) increases the number of terminal deoxynucleotidyltransferase-mediated dUTP nick end labeling (TUNEL) positive nuclei in mice 4 days post injection.