Divalent cations have a strong impact on the properties of phospholipid membranes, where amyloid-β peptides exert effects related to possible functional or pathological roles. In this work, we use an atomistic computational model of dimyristoyl-phosphatidylcholine (DMPC) membrane bilayers. We perturb this model with a simple model of divalent cations (Mg2+) and with a single amyloid-β (Aβ) peptide of 42 residues, both with and without a single Cu2+ ion bound to the N-terminus. In agreement with the experimental results reported in the literature, the model confirms that divalent cations locally destabilize the DMPC membrane bilayer and, for the first time, that the monomeric form of Aβ helps in avoiding the interactions between divalent cations and DMPC, preventing significant effects on the DMPC bilayer properties. These results are discussed in the frame of a protective role of the diluted Aβ peptide floating around phospholipid membranes.
Computational Model to Unravel the Function of Amyloid-β Peptides in Contact with a Phospholipid Membrane
La Penna G;
2020
Abstract
Divalent cations have a strong impact on the properties of phospholipid membranes, where amyloid-β peptides exert effects related to possible functional or pathological roles. In this work, we use an atomistic computational model of dimyristoyl-phosphatidylcholine (DMPC) membrane bilayers. We perturb this model with a simple model of divalent cations (Mg2+) and with a single amyloid-β (Aβ) peptide of 42 residues, both with and without a single Cu2+ ion bound to the N-terminus. In agreement with the experimental results reported in the literature, the model confirms that divalent cations locally destabilize the DMPC membrane bilayer and, for the first time, that the monomeric form of Aβ helps in avoiding the interactions between divalent cations and DMPC, preventing significant effects on the DMPC bilayer properties. These results are discussed in the frame of a protective role of the diluted Aβ peptide floating around phospholipid membranes.File | Dimensione | Formato | |
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J. Phys. Chem. B 2020, 124, 16, 3300–3314.pdf
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Descrizione: “This document is the Accepted Manuscript version of a Published Work that appeared in final form in The Journal of Physical Chemistry B, copyright © 2020 American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://doi.org/10.1021/acs.jpcb.0c00771.”
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