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J Chem Phys. 2018 Jan 28;148(4):045105. doi: 10.1063/1.5018459.

Influence of electric field on the amyloid-β(29-42) peptides embedded in a membrane bilayer.

Author information

1
School of Physics and Optoelectronic Engineering, Xidian University, Xi'an 710071, China.
2
Department of Physics, Wake Forest University, Winston-Salem, North Carolina 27106, USA.
3
Laboratoire de Biochimie Théorique, Institut de Biologie Physico-Chimique (IBPC), UPR9080 CNRS, Université Paris Diderot, Sorbonne Paris Cité, 13 Rue Pierre et Marie Curie, 75005 Paris, France.

Abstract

Alzheimer's disease is linked to various types of aggregates of amyloid-β (Aβ) peptide and their interactions with protein receptors and neuronal cell membranes. Little is known on the impact of the electric field on membrane-embedded Aβ. Here we use atomistic molecular dynamics simulations to study the effects of a constant electric field on the conformations of Aβ29-42 dimer inside a membrane, where the electric field has a strength of 20 mV/nm which exists across the membrane of a human neuron. Starting from α-helix peptides, the transmembrane electric field (TMEF) accelerates the conversion from the Gly-out substate to the Gly-side and Gly-in substates. Starting from β-sheet peptides, TMEF induces changes of the kink and tilt angles at Gly33 and Gly37. Overall, in the simulations totaling 10 μs, TMEF establishes new ground states for the dimer, similar to induced-fit in ligand binding. Our findings indicate that TMEF can stabilize rare conformations of amyloid peptides, and this could influence the cleavage of the amyloid precursor protein and the formation of β-sheet oligomers in membrane bilayers.

PMID:
29390813
DOI:
10.1063/1.5018459
[Indexed for MEDLINE]

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