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The amyloid-β (Aβ) aggregation within the brain has been from the development of Alzheimer's disease infection (AD). The earlier studies have stated that Piedmont mutation (L34V) increases the rate of Aβ40 aggregation. However, the root molecular device associated with the effectation of L34V mutation on Aβ40 structure, dynamics, and aggregation continues to be mainly ambiguous. In our study, molecular dynamics (MD) simulations were carried out to elucidate the result of
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