Effect of amyloid beta peptides Aβ<inf>1-28</inf> and Aβ<inf>25-40</inf> on model lipid membranes

Maksim Ionov, Barbara Klajnert, Konstantinos Gardikis, Sophia Hatziantoniou, Bartlomiej Palecz, Bakhtiyar Salakhutdinov, Josep Cladera, Maria Zamaraeva, Costas Demetzos, Maria Bryszewska

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28 Citations (Scopus)


To investigate the molecular interaction of amyloid beta peptides Aβ1-28 or Aβ25-40 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 (ΔH) of model lipid membranes composed of DMPC/DPPG on addition of Aβ25-40 or Aβ25-40 at 10:1 (w/w) phospholipid/peptide ratio either non-aggregated or previously aggregated were examined. The effect of Aβ1-28 and Aβ25-40 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 Aβ1-28 preferentially interacts with the hydrophilic part of the model membranes, while Aβ25-40 rather locates itself in the hydrophobic core of the bilayer where it reduces the order of the phospholipids packing. © 2009 Akadémiai Kiadó, Budapest, Hungary.
Original languageEnglish
Pages (from-to)741-747
JournalJournal of Thermal Analysis and Calorimetry
Issue number3
Publication statusPublished - 1 Mar 2010


  • Amyloid beta peptides
  • DMPC membrane
  • DPH fluorescence anisotropy
  • DSC


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