Preferential accumulation of Aβ(1−42) on gel phase domains of lipid bilayers: an AFM and fluorescence study

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DOIResolve DOI: http://doi.org/10.1016/j.bbamem.2006.09.005
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TypeArticle
Journal titleBiochimica et Biophysica Acta (BBA): Biomembranes
ISSN0005-2736
Volume1768
Issue1
Pages146154; # of pages: 9
Subjectβ-amyloid peptide; Atomic force microscopy; Bilayers; Fluourescence
AbstractPeptide-membrane interactions have been implicated in both the toxicity and aggregation of [beta]-amyloid (A[beta]) peptides. Recent studies have provided evidence for the involvement of liquid-ordered membrane domains known as lipid rafts in the formation and aggregation of A[beta]. As a model, we have examined the interaction of A[beta](1-42)?with phase separated DOPC/DPPC lipid bilayers using a combination of atomic force microscopy (AFM) and total internal reflection fluorescence microscopy (TIRF). AFM images show that addition of A[beta]?to preformed supported bilayers leads to accumulation of small peptide aggregates exclusively on the gel phase DPPC domains. Initial aggregates are observed approximately 90?min after peptide addition and increase in diameter to 45-150?nm within 24?h. TIRF studies with a mixture of A[beta] and A[beta]-Fl demonstrate that accumulation of the peptide on the gel phase domains occurs as early as 15?min after A[beta] addition and is maintained for over 24?h. By contrast, A[beta] is randomly distributed throughout both fluid and gel phases when the peptide is reconstituted into DOPC/DPPC vesicles prior to formation of a supported bilayer. The preferential accumulation of A[beta] on DPPC domains suggests that rigid domains may act as platforms to concentrate peptide and enhance its aggregation and may be relevant to the postulated involvement of lipid rafts in modulating A[beta] activity in vivo.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada; NRC Steacie Institute for Molecular Sciences; NRC Institute for Biological Sciences; NRC Canadian Neutron Beam Centre
Peer reviewedNo
Identifier10356629
NPARC number12328620
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Record identifierf7f3f6ff-e9e5-4d39-903a-22e5f1e8e8dc
Record created2009-09-10
Record modified2016-05-09
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