ArticleBiophysical journal2008
Effects of amyloid beta-peptides on the lysis tension of lipid bilayer vesicles containing oxysterols.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 36 citations in OpenAlex.
- The Structure of Oxysterols Determines Their Behavior at Phase Boundaries: Implications for Model Membranes and Structure-Activity Relationships.Advances in experimental medicine and biology · 2024Review
- TAT-RHIM: a more complex issue than expected.The Biochemical journal · 2022Article
- Imaging Flow Cytometry Illuminates New Dimensions of Amyloid Peptide-Membrane Interactions.Biophysical journal · 2020Article
- Hemoglobin S and C affect biomechanical membrane properties ofCommunications biology · 2019Article
- A silver lining for 24-hydroxycholesterol in Alzheimer's disease: The involvement of the neuroprotective enzyme sirtuin 1.Redox biology · 2018Article
- Strikingly different effects of cholesterol and 7-ketocholesterol on lipid bilayer-mediated aggregation of amyloid beta (1-42).Biochemistry and biophysics reports · 2018Article
- Frontiers of Complex Disease Mechanisms: Membrane Surface Tension May Link Genotype to Phenotype in Glaucoma.Frontiers in cell and developmental biology · 2018Article
- Phase behavior of supported lipid bilayers: A systematic study by coarse-grained molecular dynamics simulations.The Journal of chemical physics · 2017Article
- Amyloid beta oligomers induce neuronal elasticity changes in age-dependent manner: a force spectroscopy study on living hippocampal neurons.Scientific reports · 2016Article
- Influence of Global and Local Membrane Curvature on Mechanosensitive Ion Channels: A Finite Element Approach.Membranes · 2016Article
- Formation of Giant Unilamellar Proteo-Liposomes by Osmotic Shock.Langmuir : the ACS journal of surfaces and colloids · 2015Article
- Oxidized cholesterol as the driving force behind the development of Alzheimer's disease.Frontiers in aging neuroscience · 2015Review
- Biophysical insights into how surfaces, including lipid membranes, modulate protein aggregation related to neurodegeneration.Frontiers in neurology · 2013Article
- Article
- Impacts of membrane biophysics in Alzheimer's disease: from amyloid precursor protein processing to aβ Peptide-induced membrane changes.International journal of Alzheimer's disease · 2011Article
- Oxysterol-induced rearrangement of the liquid-ordered phase: a possible link to Alzheimer's disease?Journal of the American Chemical Society · 2009Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Amyloid beta-peptides (Abeta) applied directly from solution to model lipid membranes produced dramatic changes in the material properties of the bilayer when certain oxysterols were present in the bilayer. These effects were dependent on both lipid and peptide composition, and occurred at peptide concentrations as low as 100 nM. Using micropipette manipulation of giant unilamellar vesicles, we directly measured the lysis tension of lipid bilayers of various compositions. The glycerophospholipid 1-stearoyl-2-oleoyl-sn-glycero-3-phosphocholine (SOPC) constituted the main lipid component at 70 mol %. The remaining 30 mol % was composed of the following pure or mixed sterols: cholesterol (CHOL), 7-ketocholesterol (KETO), or 7beta-hydroxycholesterol (OHCHOL). SOPC/CHOL bilayers did not exhibit significant changes in mechanical properties after exposure to either Abeta(1-42) or Abeta(1-40). Partial substitution of CHOL with KETO (5 mol %), however, caused a drastic reduction of the lysis tension after exposure to Abeta(1-42) but not to Abeta(1-40). Partial substitution of CHOL with OHCHOL (5 mol %) caused a drastic reduction of the lysis tension after exposure to Abeta(1-40) and to Abeta(1-42). We attribute these effects to the reduction in intermolecular cohesive interactions caused by the presence of the second dipole of oxysterols, which reduces the energetic barrier for Abeta insertion into the bilayer.
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