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Your search keyword '"Ruysschaert, Jean-Marie"' showing total 10 results
Start Over Author "Ruysschaert, Jean-Marie" Journal biochemical journal
10 results on '"Ruysschaert, Jean-Marie"'

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

Author

Cerf E, Sarroukh R, Tamamizu-Kato S, Breydo L, Derclaye S, Dufrêne YF, Narayanaswami V, Goormaghtigh E, Ruysschaert JM, and Raussens V

Subjects
Alzheimer Disease metabolism, Amino Acid Sequence, Amyloid beta-Peptides metabolism, Humans, Molecular Sequence Data, Peptide Fragments metabolism, Protein Folding, Protein Structure, Secondary, Spectroscopy, Fourier Transform Infrared, Amyloid beta-Peptides chemistry, Peptide Fragments chemistry
Abstract

AD (Alzheimer's disease) is linked to Abeta (amyloid beta-peptide) misfolding. Studies demonstrate that the level of soluble Abeta 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 Abeta oligomers or fibrils, suggesting that structural differences between these forms of Abeta exist. Using conditions which yield well-defined Abeta-(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 Abeta was organized in a parallel beta-sheet conformation, oligomeric Abeta displayed distinct spectral features, which were attributed to an antiparallel beta-sheet structure. We also noted striking similarities between Abeta 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 Abeta oligomers, which may be related to reported effects of these highly toxic species in the amyloid pathogenesis associated with AD.

Published
2009
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