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al monoclonal antibodies have since been shown to clear plaques in mouse models but all have failed to provide benefit to people with AD in trials. The amyloid-β (Aβ) peptides aggregate into plaques contribute to the pathogenesis of AD. There are currently more than 400 trials in people of potential treatments for around the world, but almost no drugs have been brought to the market. Common mouse models of Alzheimer disease. Aggregational and conformational changes of human Aβ peptides into unique S-shaped β-sheet misfolded proteins is a pathological hallmark of neurodegenerative diseases such as AD [1]. The formation of a GM1 cluster was suggested to be cholesterol-dependent [2,3]. It was demonstrated by Matsuzaki that a GM1-including membrane not only enhanced the aggregation of Aβ but also converted amyloid peptides into toxic fibrils that showed high hydrophobicity and contained anti-parallel β-sheets [4] (Figure 1). Residue Arg5 (Figure 2) was observed to play a key role for Aβ stable binding to the membrane in the simulations [1]. Three amino acid differences distinguish Aβ from its human homolog (hAβ) and mice (mAβ) which are located within the N-terminal domain (Figure 1; Arg-5→Gly, Tyr-10→Phe, and His-13→Arg) ; however Arg-5→Gly amino acid

Why Every Year Several New Cancer Drugs Go to Market but There is no Cure Medicine for Alzheimer's? are We Off-Target?