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Biophys. J. BioFAST: First Published March 24, 2006. doi:10.1529/biophysj.105.076927
© 2006 by the Biophysical Society.

A more recent version of this article appeared on June 15, 2006.
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Anant K. Paravastu
Aneta T. Petkova
Robert Tycko
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SUPRAMOLECULAR ASSEMBLIES

Polymorphic Fibril Formation by Residues 10-40 of the Alzheimer's {beta}-Amyloid Peptide

Anant K. Paravastu 1, Aneta T. Petkova 2 and Robert Tycko 1*

1 National Institutes of Health
2 University of Florida, Gainesville

* To whom correspondence should be addressed. E-mail: robertt{at}niddk.nih.gov.

Submitted on October 31, 2005
Revised on December 21, 2005
Accepted on 27 January 2006


  Abstract
We report investigations of the morphologies and molecular structures 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 {beta}-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 morphologies were analyzed by atomic force and electron microscopies, and secondary structures and inter-sidechain proximities 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.

Key Words: Alzheimer's disease, amyloid fibril, atomic force microscopy, electron microscopy, molecular structure, solid state nuclear magnetic resonance




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Copyright © 2006 by the Biophysical Society.