Aggregation of A beta(25-35) on DOPC and DOPC/DHA Bilayers: An Atomic Force Microscopy Study (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• Aggregation of A beta(25-35) on DOPC and DOPC/DHA Bilayers: An Atomic Force Microscopy Study (Articolo in rivista) (literal)

Anno

• 2014-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1371/journal.pone.0115780 (literal)

Alternative label

• Saponetti, Matilde Sublimi; Grimaldi, Manuela; Scrima, Mario; Albonetti, Cristiano; Nori, Stefania Lucia; Cucolo, Annamaria; Bobba, Fabrizio; D'Ursi, Anna Maria (2014)
  Aggregation of A beta(25-35) on DOPC and DOPC/DHA Bilayers: An Atomic Force Microscopy Study
  in PloS one
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Saponetti, Matilde Sublimi; Grimaldi, Manuela; Scrima, Mario; Albonetti, Cristiano; Nori, Stefania Lucia; Cucolo, Annamaria; Bobba, Fabrizio; D'Ursi, Anna Maria (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 9 (literal)

Rivista

• PloS one (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali

• 18 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

• 12 (literal)

Note

• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• University of Salerno; University of Salerno; Italian Natl Res Council; University of Salerno; University of Salerno; Italian Natl Res Council (literal)

Titolo

• Aggregation of A beta(25-35) on DOPC and DOPC/DHA Bilayers: An Atomic Force Microscopy Study (literal)

Abstract

• beta 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 beta(25-35) aggregation on hydrophobic dioleoylphosphatidylcholine (DOPC) and DOPC/docosahexaenoic 22:6 acid (DHA) lipid bilayers. A beta(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 beta(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. (literal)

Prodotto di

• Istituto per lo studio dei materiali nanostrutturati (ISMN) (Istituto)

Autore CNR

• CRISTIANO ALBONETTI (Unità di personale interno)

Incoming links:

Prodotto

• Istituto per lo studio dei materiali nanostrutturati (ISMN) (Istituto)

Autore CNR di

• CRISTIANO ALBONETTI (Unità di personale interno)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• PloS one (Rivista)