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Broersen et al. Alzheimer’s Research Therapy 2010, 2:12 /content/2/4/12 R E V I E W The culprit behind amyloid beta peptide related neurotoxicity in Alzheimer’s disease: oligomer size or conformation? Kerensa Broersen, Frederic Rousseau and Joost Schymkowitz* Aβ containing plaques in the brain and the severity of the Abstract neurodegenerative symptoms observed in AD patients Since the reformulation of the amyloid cascade [5]. h erefore, the focus of research in this area has hypothesis to focus on oligomeric aggregates of shifted from senile plaques toward soluble oligomeric amyloid beta as the prime toxic species causing conformations of Aβ as the toxic species as these strongly Alzheimer’s disease, many researchers refocused on correlate with the severity of dementia [2,6,7]. h is detecting a specii c molecular assembly of dei ned oligomeric form of Aβ is highly toxic to the brain and is size that is the main trigger of Alzheimer’s disease. The the trigger for loss of synapses and neuronal damage result has been the identii cation of a host of molecular [8,9]. Because of this, many laboratories have been hunt- assemblies containing from two up to a hundred ing for a specifi c molecular assembly of defi ned size that molecules of the amyloid beta peptide, which were is the main trigger of AD. h e result has been the all found to impair memory formation in mice. This identifi cation of a host of molecular species of Aβ, clearly demonst