This study was conducted by a group of researchers at the Institute for Computational Science and Technology: Mr. Nguyen Hoang Linh, Ms. Tran Thi Minh Thu and his colleagues Mr. Ly Anh Tu, Mr. Chin-Kun Hu, and Prof. Mai Xuan Ly. It was published in the Journal of Physical Chemistry on April 17, 2017, with an impact factor (IF) of 3.2.
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Alzheimer’s disease (AD) is a chronic neurodegenerative disease that usually starts slowly and worsens over time. The most common symptoms are a difficulty in remembering recent events,1 problems with language,2 and visual−spatial search,3 among other side-effects. There exist three main hypotheses about the AD etiology, involving the tau protein, amyloid cascade, and cholinergic hypotheses.4,5 However, recent accumulated evidence strongly supports the second hypothesis, which posits that the self-assembly of amyloid β (Aβ) peptides is the main cause of AD.6,7 As Aβ peptides are proteolytic byproducts of the amyloid precursor protein, one of the strategies to treat AD is to prevent production of Aβ peptides, which are commonly composed of 40 (Aβ40) and 42 (Aβ42) amino acids.
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In the monomer state, Aβ peptides are mostly a statistical coil (SC) in physiological buffers, but aggregate to form fibrils with a β-sheet structure.8−11 Aβ42 is the dominant protein component of parenchymal plaques.12−14 Increasing the amount of Aβ42, or the concentration ratio of Aβ42/Aβ40, is associated with an increased risk of AD.15,16 In vitro studies showed that Aβ42 displays fibril nucleation and elongation rates that are higher than those of Aβ40,17 and that Aβ42 forms larger oligomers than does Aβ40.18−20 Moreover, neither the mature fibrils nor monomers of Aβ peptides are toxic; however, the esthetic of the cerebral defects in AD rather correlates with high levels of oligomers in the brain.21 This leads to the second strategy to cope with AD that is based on preventing or reversing formation of toxic oligomers,4 requiring a deep understanding of Aβ structures and self-assembly pathways.
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