Real-time monitoring of the aggregation of Alzheimer's amyloid-β via 1H magic angle spinning NMR spectroscopy

被引：32

作者：

Wang, Jian ^{[1
,2
]}

Yamamoto, Tomoya ^{[1
,2
]}

Bai, Jia ^{[1
,2
]}

Cox, Sarah J. ^{[2
]}

Korshavn, Kyle J. ^{[1
,2
]}

Monette, Martine ^{[3
]}

Ramamoorthy, Ayyalusamy ^{[1
,2
]}

机构：

[1] Univ Michigan, Biophys Program, Ann Arbor, MI 48109 USA

[2] Univ Michigan, Dept Chem, Ann Arbor, MI 48109 USA

[3] Bruker Canada Ltd, 2800 High Point Dr, Milton, ON L9T 5G5, Canada

来源：

CHEMICAL COMMUNICATIONS | 2018年 / 54卷 / 16期

关键词：

DISEASE; PROTEIN; OLIGOMERS; KINETICS; GROWTH; RESOLUTION; MECHANISM; TOXICITY; INSIGHTS; FIBRILS;

D O I：

10.1039/c8cc00167g

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Proton magic-angle-spinning NMR used for real-time analysis of amyloid aggregation reveals that mechanical rotation of A beta(1-40) monomers increases the rate of formation of aggregates, and that the increasing lag-time with peptide concentration suggests the formation of growth-incompetent species. EGCG's ability to shift off-pathway aggregation is also demonstrated.

引用

页码：2000 / 2003

页数：4

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