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

Autor: Rosenman, David J., Clemente, Nicolina, Ali, Muhammad, García, Angel E., Wang, Chunyu
Předmět:
Zdroj: Chemical Communications; 5/4/2018, Vol. 54 Issue 36, p4609-4612, 4p
Abstrakt: 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. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index