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High pressure NMR reveals conformational perturbations by disease-causing mutations in amyloid β-peptide

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Abstract

Here we present the high pressure NMR characterization of Aβ42 and two Aβ40 variants with Alzheimer-causing mutations E22G and D23N. While chemical shifts only identified localized changes at ambient pressure compared with Aβ40, high pressure NMR revealed a common site with heightened pressure sensitivity at Q15, K16 and L17 in all three variants, which correlates to higher β-propensity at central hydrophobic cluster (CHC) and faster aggregation.

Graphical abstract: High pressure NMR reveals conformational perturbations by disease-causing mutations in amyloid β-peptide

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Publication details

The article was received on 28 Feb 2018, accepted on 12 Apr 2018 and first published on 12 Apr 2018


Article type: Communication
DOI: 10.1039/C8CC01674G
Citation: Chem. Commun., 2018, Advance Article
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    High pressure NMR reveals conformational perturbations by disease-causing mutations in amyloid β-peptide

    D. J. Rosenman, N. Clemente, M. Ali, A. E. García and C. Wang, Chem. Commun., 2018, Advance Article , DOI: 10.1039/C8CC01674G

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