AI Article Synopsis
- High pressure NMR was used to study Aβ42 and Aβ40 protein variants with mutations linked to Alzheimer’s disease, specifically E22G and D23N.
- At normal pressure, only minor changes were detected in the chemical shifts of the proteins, but high pressure NMR revealed significant sensitivity at the Q15, K16, and L17 positions across all variants.
- The findings indicate that this pressure-sensitive area is associated with increased β-sheet structure and faster protein aggregation, which are important factors in Alzheimer's disease progression.
Article 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.
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| http://dx.doi.org/10.1039/c8cc01674g | DOI Listing |
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