Add Add to Quick Collection

Please use this identifier to cite or link to this item :

Antiparallel beta-sheet: a signature structure of the oligomeric amyloid beta-peptide



Abstract: AD (Alzheimer's disease) is linked to A beta (amyloid beta-peptide) misfolding. Studies demonstrate that the level Of Soluble A beta oligomeric forms correlates better with the progression of the disease than the level of fibrillar forms. Conformation-dependent antibodies have been developed to detect either A beta oligomers or fibrils, suggesting that structural differences between these forms of At exist. Using conditions which yield well-defined A beta (1-42) oligomers or fibrils, We studied the secondary structure of these species by ATR (attenuated total reflection)-FTIR (Fourier-transform infrared) spectroscopy. Whereas fibrillar A beta was organized in a parallel beta-sheet conformation, oligomeric A beta displayed distinct spectral features, which were attributed to an antiparallel beta-sheet structure. We also noted striking similarities between A beta oligomers spectra and those of bacterial outer membrane porins. We discuss our results in terms of a possible organization of the antiparallel beta-sheets in A beta oligomers, which may be related to reported effects of these highly toxic species in the amyloid pathogenesis associated with AD.

Informations complémentaires

: Accès restreint
Publication Date : 2009
Document type : Article de périodique (Journal article) - (Article de recherche)
Source : "Biochemical Journal" - Vol. 421, p. 415-423 (2009)
Peer-reviewed :
Publisher : Portland Press Ltd (London)
issn : 0264-6021
e-issn : 1470-8728
Publication status : Publié
Subject : Alzheimer's disease ; amyloid beta-peptide ; antiparallel beta-sheet ; infrared spectroscopy ; oligomeric A beta ; OmpF


Handle :
File Size Access
PDF_01 1042 - Dufrene-Cerf- 2009 -1 bytes restricted  [ucl:protected] Request copy
  • MODS
  • PDF_01
  • Close
    Articles de périodique
    Articles de périodique Antiparallel beta-sheet: a signature structure of the oligomeric amyloid beta-peptide