Jump to main content
Jump to site search
PLANNED MAINTENANCE Close the message box

Scheduled maintenance work on Wednesday 21st October 2020 from 07:00 AM to 07:00 PM (BST).

During this time our website performance may be temporarily affected. We apologise for any inconvenience this might cause and thank you for your patience.


Issue 41, 2017
Previous Article Next Article

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

Author affiliations

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

Back to tab navigation

Supplementary files

Article information


Submitted
07 Aug 2017
Accepted
26 Sep 2017
First published
27 Sep 2017

Phys. Chem. Chem. Phys., 2017,19, 27930-27934
Article type
Communication

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, 19, 27930
DOI: 10.1039/C7CP05339H

Social activity

Search articles by author

Spotlight

Advertisements