Maturation of amyloid β fibrils alters their molecular stability

被引：2

作者：

Becker, Stefan ^{[3
]}

Giller, Karin ^{[3
]}

Sieme, Daniel ^{[3
]}

Rezaei-Ghaleh, Nasrollah ^{[1
,2
]}

机构：

[1] Heinrich Heine Univ Dusseldorf, Inst Phys Biol, Univ Str 1, D-40225 Dusseldorf, Germany

[2] Forschungszentrum Julich, Inst Biol Informat Proc, IBI 7 Struct Biochem, D-52428 Julich, Germany

[3] Max Planck Inst Multidisciplinary Sci, Dept NMR Based Struct Biol, Fassberg 11, D-37077 Gottingen, Germany

来源：

PHYSICAL CHEMISTRY CHEMICAL PHYSICS | 2023年 / 25卷 / 22期

关键词：

HUMAN BRAIN; DISSOCIATION; POLYMORPHISM; HYDRATION; DYNAMICS; PROVIDES;

D O I：

10.1039/d3cp01276j

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Little is known about how maturation of Alzheimer's disease-related amyloid beta (A beta) fibrils alters their stability and potentially influences their spreading in the brain. Using high-pressure NMR, we show that progression from early to late A beta 40 aggregates enhances the kinetic stability, while ageing during weeks to months enhances their thermodynamic stability.

引用

收藏

页码：15099 / 15103

页数：5

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