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Intracerebroventricular Injection of Amyloid-β Peptides in Normal Mice to Acutely Induce Alzheimer-like Cognitive Deficits
Published on: March 16, 2016
Structural Interconversion in Alzheimer's Amyloid-β(16-35) Peptide in an Aqueous Solution
Nelson A Alves1, Rafael B Frigori2
1Departamento de Fı́sica, FFCLRP, Universidade de São Paulo , Avenida Bandeirantes, 3900, Ribeirão Preto 14040-901, SP, Brazil.
Abstract:
Structural properties of Aβ(16-35) fragment are investigated as a model for the amyloid-β peptide excluding its coil-inducing terminals. Our replica-exchange molecular dynamics simulations using all-atom and explicit aqueous solvation widely reduce any structural bias. The principal folding pathway shows direct conversion of coil to β-sheet, without the long proposed helix intermediates. Our principal component analysis indicates that the fragment is also intrinsically disordered, as the full amyloid-β peptide. Thus, the observed folding mechanism lacks free-energy barriers and any peaks in the thermal capacity.
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