Aβ structure and aggregation

Abstract

The structure of Aβ aggregates and the pathways of aggregation remains a challenging problem, although considerable progress has been made in recent years. Exact register parallelism is emerging as a common structural motif for amyloid fibrils and may also represent a key organizing principle for amyloid oligomers. Also, characterization of the interactions of Aβ with transition metals has opened up a new vista of potential pathogenic interactions and structural consequences that also may impact upon the disease state. These new insights into the structures and pathways of aggregation may help to understand the mechanisms of amyloid pathogenesis in degenerative diseases and ultimately lead to new therapeutic strategies that prevent the formation of toxic aggregates or interfere with the mechanism of toxicity. © 2007 Springer Science+Business Media, LLC. All rights reserved.