Kinetics of amyloid beta monomer-to-oligomer exchange by NMR relaxation.

ABSTRACT: Recent studies have implicated non-fibrillar oligomers of the amyloid beta (Abeta) peptide as the primary toxic species in Alzheimer's disease. Detailed structural and kinetic characterization of these states, however, has been difficult. Here we use NMR relaxation measurements to address the kinetics of exchange between monomeric and large, polymorphic oligomeric species of Abeta(1-40). (15)N and (1)H(N) R(2) data at multiple magnetic fields were recorded for several peptide concentrations subsequent to the establishment of a stable pseudo-equilibrium between monomeric and NMR-invisible soluble oligomeric species. The increase in (15)N and (1)H(N) R(2) rates as a function of protein concentration is independent of nucleus and magnetic field and shows only a small degree of variation along

SUBMITTER: Fawzi NL 

PROVIDER: S-EPMC2915839 | biostudies-literature | 2010 Jul

REPOSITORIES: biostudies-literature