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Interaction with prefibrillar species and amyloid-like fibrils changes the stiffness of lipid bilayers

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Abstract

Evaluating the toxicity of self-assembled protein states is a key step towards developing effective strategies against amyloidogenic pathologies such as Alzheimer's and Parkinson's diseases. Such analysis is directly connected to quantitatively probing the stability of the cellular membrane upon interaction with different protein states. Using a combination of spectroscopic techniques, morphological observations, and spectral analysis of membrane fluctuations, we identify different destabilisation routes for giant unilamellar vesicles interacting with native-like states, prefibrillar species and amyloid-like fibrils of α-lactalbumin. These effects range from substantially lowering the bending rigidity of the membranes to irreversible structural changes and complete disruption of the lipid bilayers. Our findings clearly indicate how the wide heterogeneity in structures occurring during protein aggregation can result in different destabilisation pathways, acting on different length scales and not limited to enhanced membrane permeability.

Graphical abstract: Interaction with prefibrillar species and amyloid-like fibrils changes the stiffness of lipid bilayers

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Publication details

The article was received on 07 Aug 2017, accepted on 26 Sep 2017 and first published on 27 Sep 2017


Article type: Communication
DOI: 10.1039/C7CP05339H
Citation: Phys. Chem. Chem. Phys., 2017, Advance Article
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    Interaction with prefibrillar species and amyloid-like fibrils changes the stiffness of lipid bilayers

    B. C. Borro, L. Parolini, P. Cicuta, V. Foderà and L. Di Michele, Phys. Chem. Chem. Phys., 2017, Advance Article , DOI: 10.1039/C7CP05339H

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