Designing conditions for in vitro formation of amyloid protofilaments and fibrils
نویسندگان
چکیده
منابع مشابه
Designing conditions for in vitro formation of amyloid protofilaments and fibrils.
We have been able to convert a small alpha/beta protein, acylphosphatase, from its soluble and native form into insoluble amyloid fibrils of the type observed in a range of pathological conditions. This was achieved by allowing slow growth in a solution containing moderate concentrations of trifluoroethanol. When analyzed with electron microscopy, the protein aggregate present in the sample aft...
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The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions.
The L55P transthyretin (TTR) familial amyloid polyneuropathy-associated variant is distinct from the other TTR variants studied to date and the wild-type protein in that the L55P tetramer can dissociate to the monomeric amyloidogenic intermediate and form fibril precursors under physiological conditions (pH 7.0, 37 degrees C). The activation barrier associated with L55P-TTR tetramer dissociatio...
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Deciphering the mechanism(s) of β-sheet mediated self-assembly is essential for understanding amyloid fibril formation and for the fabrication of polypeptide materials. Herein, we report a simple peptidomimetic that self-assembles into polymorphic β-sheet quaternary structures including protofilaments, filaments, fibrils, and ribbons that are reminiscent of the highly ordered structures display...
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The aggregation and deposition of amyloid-β((1-42) )(Aβ(42)) in the brain is implicated in the aetiology of Alzheimer's disease (AD). While the mechanism underlying its deposition in vivo is unknown its precipitation in vitro is influenced by metal ions. For example, Aβ(42) is known to bind copper, Cu(II), in vitro and binding results in aggregation of the peptide. The biophysical properties of...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1999
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.96.7.3590