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Unread 07-06-2018, 09:40 AM
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Default High pressure NMR reveals conformational perturbations by disease-causing mutations in amyloid ?-peptide.

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

Related Articles High pressure NMR reveals conformational perturbations by disease-causing mutations in amyloid ?-peptide.

Chem Commun (Camb). 2018 May 01;54(36):4609-4612

Authors: Rosenman DJ, Clemente N, Ali M, García AE, Wang C

Abstract
Here we present the high pressure NMR characterization of A?42 and two A?40 variants with Alzheimer-causing mutations E22G and D23N. While chemical shifts only identified localized changes at ambient pressure compared with A?40, high pressure NMR revealed a common site with heightened pressure sensitivity at Q15, K16 and L17 in all three variants, which correlates to higher ?-propensity at central hydrophobic cluster (CHC) and faster aggregation.


PMID: 29670961 [PubMed - indexed for MEDLINE]



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