Dynamics and Cleavability at the {alpha}-Cleavage Site of APP(684-726) in Different Lipid Environments.

Dynamics and Cleavability at the {alpha}-Cleavage Site of APP(684-726) in Different Lipid Environments. Research Abstract Details 

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Dynamics and Cleavability at the {alpha}-Cleavage Site of APP(684-726) in Different Lipid Environments. Abstract Text:

The occurrence of late-onset Alzheimer's disease has been related to the lipid homeostasis. We tested whether the membrane lipid environment affects the dynamics and cleavability of a model peptide corresponding to the amino acid sequence 684-726 of the amyloid precursor protein APP reconstituted in liposomes. Solid-state NMR with (2)H-Ala(713), which is located within the putative transmembrane domain, suggested that the peptide observes less rotational motion in egg phosphatidylcholine (PhC) membranes than in dimyristoyl-phosphatidylcholine (DMPC) bilayers above the main phase transition temperature T(c). The residue (15)N-Ala(692), which is in the vicinity of the alpha-cleavage site, i.e., Lys(687), showed less motion after reconstitution in distearoyl-phosphatidylcholine liposomes

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Dynamics and Cleavability at the {alpha}-Cleavage Site of APP(684-726) in Different Lipid Environments. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Biophysical journal

VOLUME: 95

Page Numbers: 1460-73

Journal Abbreviation: Biophys. J.

ISSN: 1542-0086

DAY: 4

MONTH: 04

YEAR: 2008

Dynamics and Cleavability at the {alpha}-Cleavage Site of APP(684-726) in Different Lipid Environments. Information

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LANGUAGE: eng

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AFFILIATION: Institute of Pharmaceutical Sciences, and Laboratory of Physical Chemistry, ETH Zurich (Swiss Federal Institute of Technology Zurich), Switzerland.

Country: United States

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MEDLINETA: Biophys J

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