Amyloid-β Peptide Triggers Membrane Remodeling in Supported Lipid Bilayers Depending on Their Hydrophobic Thickness

Langmuir : the ACS Journal of Surfaces and Colloids
Sigalit MekerNam-Joon Cho

Abstract

Amyloid-β (Aβ) peptide has been implicated in Alzheimer's disease, which is a leading cause of death worldwide. The interaction of Aβ peptides with the lipid bilayers of neuronal cells is a critical step in disease pathogenesis. Recent evidence indicates that lipid bilayer thickness influences Aβ membrane-associated aggregation, while understanding how Aβ interacts with lipid bilayers remains elusive. To address this question, we employed supported lipid bilayer (SLB) platforms composed of different-length phosphatidylcholine (PC) lipids (C12:0 DLPC, C18:1 DOPC, C18:1-C16:0 POPC), and characterized the resulting interactions with soluble Aβ monomers. Quartz crystal microbalance-dissipation (QCM-D) experiments identified concentration-dependent Aβ peptide adsorption onto all tested SLBs, which was corroborated by fluorescence recovery after photobleaching (FRAP) experiments indicating that higher Aβ concentrations led to decreased membrane fluidity. These commonalities pointed to strong Aβ peptide-membrane interactions in all cases. Notably, time-lapsed fluorescence microscopy revealed major differences in Aβ-induced membrane morphological responses depending on SLB hydrophobic thickness. For thicker DOPC and POPC SLBs, membrane...Continue Reading

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Citations

Nov 6, 2020·Quarterly Reviews of Biophysics·Jinming WuJinghui Luo
Mar 23, 2021·Advanced Nanobiomed Research·Yuhuan LiPu Chun Ke
May 15, 2021·Macromolecular Rapid Communications·Newton SenWolfgang H Binder
Jul 3, 2021·International Journal of Molecular Sciences·Benita WiatrakKazimierz Gąsiorowski

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