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• W1570954326 abstract "The fibrillogenic peptide corresponding to the residues 106–126 of the prion protein sequence (PrP 106–126) is largely used to explore the neurotoxic mechanisms underlying the prion disease. However, whether the neuronal toxicity of PrP 106–126 is caused by a soluble or fibrillar form of this peptide is still unknown. The aim of this study was to correlate the structural state of this peptide with its neurotoxicity. Here we show that the two conserved Gly114 and Gly119 residues, in force of their intrinsic flexibility, prevent the peptide assuming a structured conformation, favouring its aggregation in amyloid fibrils. The substitution of both Gly114 and Gly119 with alanine residues (PrP 106–126 AA mutated peptide) reduces the flexibility of this prion fragment and results in a soluble, β-structured peptide. Moreover, PrP 106–126 AA fragment was highly toxic when incubated with neuroblastoma cells, likely behaving as a neurotoxic protofibrillar intermediate of the wild-type PrP 106–126. These data further confirm that the fibrillar aggregation is not necessary for the induction of the toxic effects of PrP 106–126." @default.
• W1570954326 created "2016-06-24" @default.
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• W1570954326 date "2003-03-18" @default.
• W1570954326 modified "2023-09-23" @default.
• W1570954326 title "Contribution of two conserved glycine residues to fibrillogenesis of the 106-126 prion protein fragment. Evidence that a soluble variant of the 106-126 peptide is neurotoxic" @default.
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• W1570954326 doi "https://doi.org/10.1046/j.1471-4159.2003.01664.x" @default.
• W1570954326 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12641727" @default.
• W1570954326 hasPublicationYear "2003" @default.
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