Polymorphic fibril formation by residues 10-40 of the Alzheimer's β-amyloid peptide

被引:177
作者
Paravastu, Anant K. [1 ]
Petkova, Aneta T. [1 ]
Tycko, Robert [1 ]
机构
[1] NIDDK, Chem Phys Lab, NIH, Bethesda, MD 20892 USA
关键词
D O I
10.1529/biophysj.105.076927
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
We report investigations of the morphology and molecular structure of amyloid fibrils comprised of residues 10-40 of the Alzheimer's beta-amyloid peptide (A beta(10-40)), prepared under various solution conditions and degrees of agitation. Omission of residues 1-9 from the full-length Alzheimer's b-amyloid peptide (A beta(1-40)) did not prevent the peptide from forming amyloid fibrils or eliminate fibril polymorphism. These results are consistent with residues 1-9 being disordered in A beta(1-40) fibrils, and show that fibril polymorphism is not a consequence of disorder in residues 1-9. Fibril morphology was analyzed by atomic force and electron microscopy, and secondary structure and inter-side-chain proximity were probed using solid-state NMR. A beta(1-40) fibrils were found to be structurally compatible with A beta(10-40): A beta(1-40) fibril fragments were used to seed the growth of A beta(10-40) fibrils, with propagation of fibril morphology and molecular structure. In addition, comparison of lyophilized and hydrated fibril samples revealed no effect of hydration on molecular structure, indicating that A beta(10-40) fibrils are unlikely to contain bulk water.
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收藏
页码:4618 / 4629
页数:12
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