Distinct conformational states of the Alzheimer β-amyloid peptide can be detected by high-pressure NMR spectroscopy

Abstract

Folding under pressure: High-pressure NMR spectroscopy detects three different conformational states of the Aβ-peptide in solution: a compactly folded state 1, a partially folded state 2′, and a random-coil like state 2′′ (see plot, p=population). At ambient pressure the folded state 1 dominates which probably has a high affinity to fibrils and thus may promote fibril formation.