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Structural polymorphism of Alzheimer Aβ and other amyloid fibrils

TitleStructural polymorphism of Alzheimer Aβ and other amyloid fibrils
Publication TypeJournal Article
Year of Publication2009
AuthorsFändrich, M, Meinhardt J, Grigorieff N
Refereed DesignationRefereed
JournalPrion
Volume3
Pagination89-93
Date Published06/2009
ISSN1933-6896
Abstract

Deposits of amyloid fibrils characterize a diverse group of human diseases that includes Alzheimer disease, Creutzfeldt-Jakob disease and type II diabetes. Amyloid fibrils formed from different polypeptides contain a common cross-beta spine. Nevertheless, amyloid fibrils formed from the same polypeptide can occur in a range of structurally different morphologies. The heterogeneity of amyloid fibrils reflects different types of polymorphism: (1) variations in the protofilament number, (2) variations in the protofilament arrangement and (3) different polypeptide conformations. Amyloid fibril polymorphism implies that fibril formation can lead, for the same polypeptide sequence, to many different patterns of inter- or intra-residue interactions. This property differs significantly from native, monomeric protein folding reactions that produce, for one protein sequence, only one ordered conformation and only one set of inter-residue interactions.

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