Reference : Study of the specific lipid binding properties of Abeta 11-22 fragment at endosomal pH.
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/63266
Study of the specific lipid binding properties of Abeta 11-22 fragment at endosomal pH.
English
Ravault, S. [> > > >]
Flore, Christelle [Université de Liège - ULg > > Gembloux Agro-Bio Tech >]
Saurel, O. [> > > >]
Milon, A. [> > > >]
Brasseur, Robert mailto [Université de Liège - ULg > > Gembloux Agro-Bio Tech >]
Lins, Laurence mailto [Université de Liège - ULg > > Gembloux Agro-Bio Tech >]
2009
Langmuir
American Chemical Society
25
18
10948-53
Yes (verified by ORBi)
International
0743-7463
1520-5827
Washington
DC
[en] Amino Acid Motifs ; Amino Acid Sequence ; Amyloid beta-Protein/chemistry/metabolism ; Circular Dichroism ; Endosomes/metabolism ; Histidine/metabolism ; Hydrogen-Ion Concentration ; Hydrophobicity ; Magnetic Resonance Spectroscopy ; Membranes, Artificial ; Molecular Sequence Data ; Peptide Fragments/chemistry/metabolism ; Phospholipids/metabolism ; Protein Binding ; Protein Conformation ; Solubility ; Static Electricity ; Substrate Specificity ; Unilamellar Liposomes/chemistry/metabolism
[en] Increasing evidence implicates interactions between Abeta peptide and lipids in the development of Alzheimer's disease. More generally, Abeta peptide interactions with membranes seem to depend on the composition of the lipid bilayer and the structural features of the peptide. One key parameter should be pH, since one site of intracellular Abeta peptide production and/or accumulation is likely to be endosomes. This intracellular endosomal accumulation was suggested to contribute to disease progression. In this paper, we report a study on the 11-22 amphiphilic domain of Abeta in interaction with model membrane; this region contains most of the charged residues of the N-terminal domain of Abeta. We show that the peptide charge, and more precisely the protonation state of histidines 13 and/or 14, is important for the interaction with lipids. Hence, it is only at endosomal pH that a conformational change of the peptide is observed in the presence of negatively charged lipid vesicles, that is, when both lipid headgroups and histidines can interact through electrostatic interactions. Specific interactions of the fragment with phosphatidylserine and to a lesser extent with phosphatidylcholine, but not phosphatidylethanolamine, are further evidenced by the Langmuir monolayer technique. From our results, we suggest that the protonation state of His residues could have a role in the pathogenic surface interaction of the whole Abeta peptide with membranes.
http://hdl.handle.net/2268/63266
10.1021/la901544g
Laurence Lins est dernier auteur

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