Label-free methods for probing the interaction of clioquinol with amyloid-β

被引：16

作者：

Cheng, Xin Ran ^{[2
]}

Hung, Vinci Wing Sze ^{[2
]}

Scarano, Simona ^{[1
]}

Mascini, Marco ^{[1
]}

Minunni, Maria ^{[1
]}

Kerman, Kagan ^{[2
]}

机构：

[1] Univ Florence, Dipartimento Chim Ugo Schiff, I-50019 Sesto Fiorentino, Italy

[2] Univ Toronto Scarborough, Dept Phys & Environm Sci, Toronto, ON M1C 1A4, Canada

来源：

ANALYTICAL METHODS | 2012年 / 4卷 / 08期

基金：

加拿大自然科学与工程研究理事会;

关键词：

SURFACE-PLASMON RESONANCE; ALZHEIMERS-DISEASE; TRANSGENIC MICE; ALPHA-SYNUCLEIN; IN-VITRO; AGGREGATION; PEPTIDE; PROTEIN; FIBRILS; GROWTH;

D O I：

10.1039/c2ay25123j

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

The presence of amyloid-beta (A beta) fibrils is characteristic of Alzheimer's disease (AD), and the aggregation of these amyloidogenic proteins is a nucleation-dependent process. In this report, label-free methods based on surface plasmon resonance (SPR) and thickness shear mode acoustic wave sensors (TSM-AWS) were used to detect monomer elongation in real-time. The modulation of A beta aggregation using a well-described flavonoid, clioquinol (CQ) was also observed. Established methods like fluorescence and electrochemistry were also employed to confirm the interaction of CQ with A beta. Good correlation between the designed label-free methods creates a promising platform for the screening of novel amyloid inhibitors.

引用

页码：2228 / 2232

页数：5

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