Cerf, Emilie
[Center for Structural Biology and Bioinformatics, Laboratory for Structure and Function of Biological Membranes, Faculte des Sciences, Universite Libre de Bruxelles]
Sarroukh, Rabia
[Faculte des Sciences, Universite Libre de Bruxelles]
Tamamizu-Kato, Shiori
[Martin Luther King Jr. Way, Oakland, CA 94609, U.S.A.]
Breydo, Leonid
[University of California at Irvine, 3438 McGaugh Hall, Irvine, CA 92697, U.S.A]
Derclaye, Sylvie
[UCL]
Dufrêne, Yves
[UCL]
Narayanaswami, Vasanthy
[Martin Luther King Jr. Way, Oakland, CA 94609, U.S.A.]
Goormaghtigh, Erik
[Faculte des Sciences, Universite Libre de Bruxelles]
Ruysschaert, Jean-Marie
[Faculte des Sciences, Universite Libre de Bruxelles]
Raussens, Vincent
[Faculte des Sciences, Universite Libre de Bruxelles]
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.
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Bibliographic reference
Cerf, Emilie ; Sarroukh, Rabia ; Tamamizu-Kato, Shiori ; Breydo, Leonid ; Derclaye, Sylvie ; et. al. Antiparallel beta-sheet: a signature structure of the oligomeric amyloid beta-peptide. In: Biochemical Journal, Vol. 421, p. 415-423 (2009)