Ganglioside GM1 produces stable, short, and cytotoxic Aβ40 protofibrils

被引：7

作者：

Kumar, Manjeet ^{[1
]}

Ivanova, Magdalena I. ^{[2
]}

Ramamoorthy, Ayyalusamy ^{[1
]}

机构：

[1] Univ Michigan, Michigan Neurosci Inst, Dept Chem Biomed Engn Macromol Sci & Engn, Biophys, Ann Arbor, MI 48109 USA

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

来源：

CHEMICAL COMMUNICATIONS | 2023年 / 59卷 / 46期

基金：

美国国家卫生研究院;

关键词：

AMYLOID BETA-PROTEIN; THIOFLAVIN-T-BINDING; ALZHEIMERS-DISEASE; AGGREGATION; FIBRILS; MECHANISM; MEMBRANES; FORM; SEED;

D O I：

10.1039/d3cc02186f

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Monosialoganglioside GM1-bound amyloid beta-peptides have been found in patients' brains exhibiting early pathological changes of Alzheimer's disease. Herein, we report the ability of non-micellar GM1 to modulate A beta(40) aggregation resulting in the formation of stable, short, rod-like, and cytotoxic A beta(40) protofibrils with the ability to potentiate both A beta(40) and A beta(42) aggregation.

引用

页码：7040 / 7043

页数：4

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