Stephen C. Meredith

TL;DR: All amino acids, including proline, are converted quantitatively to phenylthiocarbamyl compounds and these are stable enough to eliminate any need for in-line derivatization, providing results comparable in sensitivity and precision to those obtained by state-of-the-art ion-exchange analyzers.

TL;DR: The data suggest that fibrils in the brain may spread from a single nucleation site, that structural variations may correlate with variations in AD, and that structure-specific amyloid imaging agents may be an important future goal.

TL;DR: How the fibril structure is resolved by mapping interstrand distances in this core region of the Aβ peptide chain with solid-state NMR is reported, establishing that this central core of Aβ consists of a parallel β-sheet structure in which identical residues on adjacent chains are aligned directly, i.e., in register.

TL;DR: In this paper, 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.

TL;DR: It is demonstrated through thioflavin T fluorescence and electron microscopy that fibrils extracted from brain tissue of deceased AD patients can be used to seed the growth of synthetic Aβ1–40fibrils, allowing preparation of fibril with isotopic labeling and in sufficient quantities for solid-state NMR and other measurements.