β 淀粉样纤维的成熟会改变其分子稳定性。
Maturation of amyloid β fibrils alters their molecular stability.
机构信息
Department of NMR-based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Am Fassberg 11, D-37077 Göttingen, Germany.
Institute of Physical Biology, Heinrich Heine University Düsseldorf, Universitätsstraße 1, D-40225 Düsseldorf, Germany.
出版信息
Phys Chem Chem Phys. 2023 Jun 7;25(22):15099-15103. doi: 10.1039/d3cp01276j.
Little is known about how maturation of Alzheimer's disease-related amyloid β (Aβ) fibrils alters their stability and potentially influences their spreading in the brain. Using high-pressure NMR, we show that progression from early to late Aβ40 aggregates enhances the kinetic stability, while ageing during weeks to months enhances their thermodynamic stability.
关于阿尔茨海默病相关淀粉样 β (Aβ) 纤维的成熟如何改变其稳定性，以及如何潜在地影响其在大脑中的扩散，目前知之甚少。我们使用高压 NMR 表明，从早期到晚期 Aβ40 聚集物的进展增强了动力学稳定性，而在数周到数月的老化过程中增强了热力学稳定性。
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