Abstract:
:We report constraints on the supramolecular structure of amyloid fibrils formed by the 40-residue beta-amyloid peptide associated with Alzheimer's disease (A beta(1-40)) obtained from solid-state nuclear magnetic resonance (NMR) measurements of intermolecular dipole-dipole couplings between (13)C labels at 11 carbon sites in residues 2 through 39. The measurements are carried out under magic-angle spinning conditions, using the constant-time finite-pulse radiofrequency-driven recoupling (fpRFDR-CT) technique. We also present one-dimensional (13)C magic-angle spinning NMR spectra of the labeled A beta(1-40) samples. The fpRFDR-CT data reveal nearest-neighbor intermolecular distances of 4.8 +/- 0.5 A for carbon sites from residues 12 through 39, indicating a parallel alignment of neighboring peptide chains in the predominantly beta-sheet structure of the amyloid fibrils. The one-dimensional NMR spectra indicate structural order at these sites. The fpRFDR-CT data and NMR spectra also indicate structural disorder in the N-terminal segment of A beta(1-40), including the first nine residues. These results place strong constraints on any molecular-level structural model for full-length beta-amyloid fibrils.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Balbach JJ,Petkova AT,Oyler NA,Antzutkin ON,Gordon DJ,Meredith SC,Tycko Rdoi
10.1016/S0006-3495(02)75244-2subject
Has Abstractpub_date
2002-08-01 00:00:00pages
1205-16issue
2eissn
0006-3495issn
1542-0086pii
S0006-3495(02)75244-2journal_volume
83pub_type
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