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    Biochem Biophys Res Commun. 1997 Apr 28;233(3):760-4.

    Alzheimer's disease amyloid beta peptide 25-35 inhibits lipid peroxidation as a result of its membrane interactions.

    Walter MF, Mason PE, Mason RP.

    Source

    Laboratory for Membrane Structure Studies, MCP-Hahnemann School of Medicine, Allegheny University of the Health Sciences, Pittsburgh, Pennsylvania 15212-4772, USA.

    Abstract

    The biological activity of the Alzheimer's disease amyloid beta protein may be related to modulation of membrane lipid peroxidation. The effect of amyloid beta protein fragment 25-35 [A beta(25-35)] on lipid peroxidation was examined in liposomes enriched with polyunsaturated fatty acids. The activity of A beta(25-35) was compared to that of A beta(25-35) with either a scrambled sequence [A beta(25-35)scram] or a peptide sequence in which methionine was replaced with leucine [A beta(25-35) met]. A beta(25-35) inhibited lipid peroxidation in a dose- and time-dependent manner. The antioxidant activity of A beta(25-35) was observed at concentrations as low as 10 nM. The relative antioxidant activities of the amyloid beta protein fragments were as follows: A beta(25-35) > A beta(25-35) met > A beta(25-35)scram. The two more potent peptides intercalated into the membrane hydrocarbon core, as determined by small-angle x-ray diffraction approaches. These findings indicate that the amphiphilic A beta(25-35) peptide inhibits lipid peroxidation at low concentrations as a result of physicochemical interactions with the membrane lipid bilayer.

    PMID:
    9168929
    [PubMed - indexed for MEDLINE]

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