Abstract
The misfolding, aggregation and accumulation of proteins in the brain, represents a common feature of diverse neurodegenerative diseases among which Alzheimers disease (AD). Important therapeutic strategies for this pathology aim at inhibiting the aggregation of misfolded amyloid β (Aβ) peptides into different species, particularly intermediate oligomeric assemblies, which are believed to be the most neurotoxic species. Here we review the structural data present in the literature, with the purpose to supply useful information for the rational design of new potential molecules able to target Aβ peptides and fibrils. In particular, structural information concerning the different Aβ peptides assemblies, their supramolecular organization, their interaction with cations, biological membranes and known ligands are reported.
Keywords: neurodegenerative disease, biological membrane, heart disease, intermediate oligomeric assemblies, aggregates, β-amyloid, Aβ oligomers, Aβ fibrils, Aβ peptide structural features, Alzheimers's disease
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