Utilizing magnetic resonance techniques to study membrane interactions of amyloid peptides

被引：5
|
作者：
Rajput, Sunnia [1 ]
Sani, Marc-Antoine [1 ,2 ]
Keizer, David W. [1 ]
Separovic, Frances [1 ,2 ]
机构：
[1] Univ Melbourne, Bio21 Mol Sci & Biotechnol Inst, Melbourne, Vic 3010, Australia
[2] Univ Melbourne, Sch Chem, Melbourne, Vic 3010, Australia
来源：
BIOCHEMICAL SOCIETY TRANSACTIONS | 2021年 / 49卷 / 03期
基金：
澳大利亚研究理事会;
关键词：
IN-CELL NMR; BETA-PEPTIDE; ALZHEIMERS-DISEASE; PRECURSOR PROTEIN; ENDOGENOUS SEED; CHEMICAL-SHIFTS; AGGREGATION; MODEL; GM1; CHOLESTEROL;
D O I：
10.1042/BST20201244
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Alzheimer's disease (AD) is a common neurodegenerative condition that involves the extracellular accumulation of amyloid plaques predominantly consisting of A beta peptide aggregates. The amyloid plaques and soluble oligomeric species of A beta are believed to be the major cause of synaptic dysfunction in AD brain and their cytotoxic mechanisms have been proposed to involve interactions with cell membranes. In this review, we discuss our solid-state nuclear magnetic resonance (ssNMR) studies of A beta interactions with model membranes.
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页码：1457 / 1465
页数：9
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