Core Structure of Amyloid Fibrils Formed by Residues 106–126 of the Human Prion Protein
Copyright policy )Core Structure of Amyloid Fibrils Formed by Residues 106–126 of the Human Prion Protein
Peptides comprising residues 106-126 of the human prion protein (PrP) exhibit many features of the full-length protein. PrP(106-126) induces apoptosis in neurons, forms fibrillar aggregates, and can mediate the conversion of native cellular PrP (PrP(C)) to the scrapie form (PrP(Sc)). Despite a wide range of biochemical and biophysical studies on this peptide, including investigation of its propensity for aggregation, interactions with cell membranes, and PrP-like toxicity, the structure of amyloid fibrils formed by PrP(106-126) remains poorly defined. In this study we use solid-state nuclear magnetic resonance to define the secondary and quaternary structure of PrP(106-126) fibrils. Our results reveal that PrP(106-126) forms in-register parallel beta sheets, stacked in an antiparallel fashion within the mature fibril. The close intermolecular contacts observed in the fibril core provide a rational for the sequence-dependent behavior of PrP(106-126), and provide a basis for further investigation of its biological properties.
- University of Toronto Canada
- Hospital for Sick Children Canada
Models, Molecular, Amyloid, Protein Folding, Prions, Protein Conformation, Circular Dichroism, PROTEIN, Peptide Fragments, Structural Biology, Humans, Molecular Biology, Nuclear Magnetic Resonance, Biomolecular
Models, Molecular, Amyloid, Protein Folding, Prions, Protein Conformation, Circular Dichroism, PROTEIN, Peptide Fragments, Structural Biology, Humans, Molecular Biology, Nuclear Magnetic Resonance, Biomolecular
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