Effect of amyloid beta peptides Aβ1–28 and Aβ25–40 on model lipid membranes.

To investigate the molecular interaction of amyloid beta peptides Aβ_1–28 or Aβ_25–40 with model lipid membranes differential scanning calorimetry (DSC) and DPH and TMA DPH fluorescence anisotropy approaches were used. The main transition temperature ( T_m) and enthalpy change (Δ H) of model lipid membranes composed of DMPC/DPPG on addition of Aβ_25–40 or Aβ_25–40 at 10:1 (w/w) phospholipid/peptide ratio either non-aggregated or previously aggregated were examined. The effect of Aβ_1–28 and Aβ_25–40 on the membrane fluidity of liposomes made of DMPC/DPPG (98:2 w/w) was determined by fluorescence anisotropy of incorporated DPH and TMA DPH. The results of this study provide information that Aβ_1–28 preferentially interacts with the hydrophilic part of the model membranes, while Aβ_25–40 rather locates itself in the hydrophobic core of the bilayer where it reduces the order of the phospholipids packing. [ABSTRACT FROM AUTHOR]