Molecular architecture of Aβ fibrils grown in cerebrospinal fluid solution and in a cell culture model of Aβ plaque formation

Abstract

Our data reveal that, despite considerable variations in morphology, the spectroscopic properties and the pattern of slowly exchanging backbone amides are closely similar in the fibrils investigated. This finding implies that a fundamentally conserved molecular architecture of Aβ peptide fold is common to Aβ fibrils.

DMSO-Quenched H/D-Exchange 2D NMR Spectroscopy and Its Applications in Protein Science

“…These studies gave us information about the molecular mechanisms of amyloid formation. Although the DMSO solution based on the standard protocol is composed of 95% DMSO-d 6 at pH* 5-6 adjusted by DCA-d 2 , slightly modified compositions, e.g., dry DMSO-d 6 [103,125] and DMSO-d 6 /trifluoroacetic acid-d 1 (0.01-1%) mixture [107,110,[114][115][116][117]119,122,126,128,129] were also used as an H/D-exchange quenching solution. Several excellent review articles on the DMSO-quenched H/D-exchange method have been published and cover more details about the method [130][131][132][133][134].…”