AI Article Synopsis
- The study examines how the amyloid-β peptide interacts with lipid membranes using small angle neutron scattering and molecular dynamics simulations.
- Researchers focus on the effects of introducing negatively charged lipids (DMPS) into a membrane composed of DMPC, observing changes in membrane thickness and structure with temperature variations.
- Findings indicate that the morphological changes between different membrane structures are not influenced by the presence of charge in the system.
Article Abstract
Amyloid-β peptide interactions with model lipid membranes have been studied by means of small angle neutron scattering and molecular dynamics simulations. These interactions had been indicated recently as an origin of the membrane structure reorganizations between spherical small unilamellar vesicles and planar bicelle-like structures. In present work, we investigate the influence of charge on the peptide-triggered morphological changes by introducing the anionic lipid DMPS to the underlying DMPC membrane. Changes to the membrane thickness and the overall membrane structure with and without Aβ25-35 incorporated have been investigated over a wide range of temperatures. Our results document the previously reported morphological reformations between bicelle-like structures present in gel phase and small unilamellar vesicles present in fluid phase to be independent from the charge existence in the system.
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| http://dx.doi.org/10.4149/gpb_2022052 | DOI Listing |
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