Reference : Fusogenic Alzheimer'S Peptide Fragment A Beta (29-42) In Interaction With Lipid Bilay...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/63506
Fusogenic Alzheimer'S Peptide Fragment A Beta (29-42) In Interaction With Lipid Bilayers: Secondary Structure, Dynamics, And Specific Interaction With Phosphatidyl Ethanolamine Polar Heads As Revealed By Solid-State Nmr
English
Ravault, S. [> > > >]
Soubias, O. [> > > >]
Saurel, O. [> > > >]
Thomas, Annick [Université de Liège - ULg > Chimie et bio-industries > Centre de Bio. Fond. - Section de Biologie moléc. et numér. >]
Brasseur, Robert mailto [Université de Liège > > Gembloux Agro-Bio Tech >]
Milon, A. [> > > >]
2005
Protein Science : A Publication of the Protein Society
14
5
1181-9
Yes (verified by ORBi)
0961-8368
[en] The interaction of the native Alzheimer's peptide C-terminal fragment Abeta
(29-42), and two mutants (G33A and G37A) with neutral lipid bilayers made of POPC
and POPE in a 9:1 molar ratio was investigated by solid-state NMR. This fragment
and the lipid composition were selected because they represent the minimum
requirement for the fusogenic activity of the Alzheimer's peptide. The chemical
shifts of alanine methyl isotropic carbon were determined by MAS NMR, and they
clearly demonstrated that the major form of the peptide equilibrated in membrane
is not in a helical conformation. (2)H NMR, performed with acyl chain deuterated
POPC, demonstrated that there is no perturbation of the acyl chain's dynamics and
of the lipid phase transition temperature. (2)H NMR, performed with alanine
methyl-deuterated peptide demonstrated that the peptide itself has a limited
mobility below and above the lipid phase transition temperature (molecular order
parameter equal to 0.94). MAS (31)P NMR revealed a specific interaction with POPE
polar head as seen by the enhancement of POPE phosphorus nuclei T(2) relaxation.
All these results are in favor of a beta-sheet oligomeric association of the
peptide at the bilayer interface, preferentially recruiting phosphatidyl
ethanolamine polar heads.
Researchers ; Professionals
http://hdl.handle.net/2268/63506
10.1110/ps.041291405

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