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• W2023144502 abstract "Amyloid β-peptides (Aβ) 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 7β-hydroxycholesterol (OHCHOL). SOPC/CHOL bilayers did not exhibit significant changes in mechanical properties after exposure to either Aβ(1–42) or Aβ(1–40). Partial substitution of CHOL with KETO (5 mol %), however, caused a drastic reduction of the lysis tension after exposure to Aβ(1–42) but not to Aβ(1–40). Partial substitution of CHOL with OHCHOL (5 mol %) caused a drastic reduction of the lysis tension after exposure to Aβ(1–40) and to Aβ(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 Aβ insertion into the bilayer." @default.
• W2023144502 created "2016-06-24" @default.
• W2023144502 creator A5048618737 @default.
• W2023144502 creator A5090075416 @default.
• W2023144502 date "2008-07-01" @default.
• W2023144502 modified "2023-09-27" @default.
• W2023144502 title "Effects of Amyloid β-Peptides on the Lysis Tension of Lipid Bilayer Vesicles Containing Oxysterols" @default.
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• W2023144502 doi "https://doi.org/10.1529/biophysj.107.114983" @default.
• W2023144502 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2440435" @default.
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