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Originally published as Biophys J. BioFAST on March 24, 2006.
doi:10.1529/biophysj.105.076927
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Biophysical Journal 90:4618-4629 (2006)
© 2006 The Biophysical Society

Polymorphic Fibril Formation by Residues 10–40 of the Alzheimer's ß-Amyloid Peptide

Anant K. Paravastu, Aneta T. Petkova and Robert Tycko

Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland

Correspondence: Address reprint requests to Dr. Robert Tycko, National Insitutes of Health, Bldg. 5, Rm. 112, Bethesda, MD 20892-0520. Tel.: 301-402-8272; Fax: 301-496-0825; E-mail: robertty{at}mail.nih.gov.

We report investigations of the morphology and molecular structure of amyloid fibrils comprised of residues 10–40 of the Alzheimer's ß-amyloid peptide (Aß10–40), prepared under various solution conditions and degrees of agitation. Omission of residues 1–9 from the full-length Alzheimer's ß-amyloid peptide (Aß1–40) did not prevent the peptide from forming amyloid fibrils or eliminate fibril polymorphism. These results are consistent with residues 1–9 being disordered in Aß1–40 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. Aß1–40 fibrils were found to be structurally compatible with Aß10–40: Aß1–40 fibril fragments were used to seed the growth of Aß10–40 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 Aß10–40 fibrils are unlikely to contain bulk water.




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