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Aggregation of Aß(25-35) on DOPC and DOPC/DHA bilayers: an atomic force microscopy study.


ABSTRACT: ? amyloid peptide plays an important role in both the manifestation and progression of Alzheimer disease. It has a tendency to aggregate, forming low-molecular weight soluble oligomers, higher-molecular weight protofibrillar oligomers and insoluble fibrils. The relative importance of these single oligomeric-polymeric species, in relation to the morbidity of the disease, is currently being debated. Here we present an Atomic Force Microscopy (AFM) study of A?(25-35) aggregation on hydrophobic dioleoylphosphatidylcholine (DOPC) and DOPC/docosahexaenoic 22?6 acid (DHA) lipid bilayers. A?(25-35) is the smallest fragment retaining the biological activity of the full-length peptide, whereas DOPC and DOPC/DHA lipid bilayers were selected as models of cell-membrane environments characterized by different fluidity. Our results provide evidence that in hydrophobic DOPC and DOPC/DHA lipid bilayers, A?(25-35) forms layered aggregates composed of mainly annular structures. The mutual interaction between annular structures and lipid surfaces end-results into a membrane solubilization. The presence of DHA as a membrane-fluidizing agent is essential to protect the membrane from damage caused by interactions with peptide aggregates; to reduces the bilayer defects where the delipidation process starts.

SUBMITTER: Sublimi Saponetti M 

PROVIDER: S-EPMC4281140 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

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Aggregation of Aß(25-35) on DOPC and DOPC/DHA bilayers: an atomic force microscopy study.

Sublimi Saponetti Matilde M   Grimaldi Manuela M   Scrima Mario M   Albonetti Cristiano C   Nori Stefania Lucia SL   Cucolo Annamaria A   Bobba Fabrizio F   D'Ursi Anna Maria AM  

PloS one 20141231 12


β amyloid peptide plays an important role in both the manifestation and progression of Alzheimer disease. It has a tendency to aggregate, forming low-molecular weight soluble oligomers, higher-molecular weight protofibrillar oligomers and insoluble fibrils. The relative importance of these single oligomeric-polymeric species, in relation to the morbidity of the disease, is currently being debated. Here we present an Atomic Force Microscopy (AFM) study of Aβ(25-35) aggregation on hydrophobic diol  ...[more]

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