Solid-State NMR of Amyloid Membrane Interactions

Abstract

Solid-state NMR pulse sequences often feature fewer pulses and delays than the more common solution NMR experiments. This ostensible simplicity, however, belies the care with which experimental parameters must be determined, as solid-state NMR can be much less forgiving of improper experimental set-up. This is especially true of “semi-solid” samples, such as the phospholipid vesicles used to study membrane-associated peptides and proteins, which feature prominently in misfolding diseases. Protocols for the preparation of multilamellar vesicles for solid-state NMR studies of Aβ peptides are described, together with procedures for optimization of critical experimental parameters, such as spectral widths, delay times, and field strengths for ³¹P, ²H, and ¹³C NMR spectroscopy.