Work

Structural polymorphism of Alzheimer Aβ and other amyloid fibrils

Year: 2009

Type: review

Abstract: Deposits of amyloid fibrils characterize a diverse group of human diseases that includes Alzheimer's 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: (i) variations in the protofilament number, (ii) variations in the protofilament arrangement and (iii) 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.

Source: Prion

DOI: 10.4161/pri.3.2.8859

Authors: Marcus Fändrich, Jessica Meinhardt, Nikolaus Grigorieff

Institutions: Max Planck Research Unit for Enzymology of Protein Folding, Martin Luther University Halle-Wittenberg, Leibniz Institute on Aging - Fritz Lipmann Institute (FLI), Brandeis University

Language: English

Topic: Alzheimer's disease research and treatments

Subfield: Physiology

Field: Medicine

Domain: Health Sciences

SDG: Good health and well-being

Open Access status: bronze