Synchrotron μ-FTIR highlights amyloid-β conformational changes under the effect of surface wettability and external agents

被引：6

作者：

Accardo, Angelo ^{[1
]}

Shalabaeva, Victoria ^{[1
]}

Hesse, Bernhard ^{[2
]}

Cotte, Marine ^{[2
,3
]}

Krahne, Roman ^{[1
]}

Riekel, Christian ^{[2
]}

Dante, Silvia ^{[1
]}

机构：

[1] Ist Italian Tecnol, I-16163 Genoa, Italy

[2] European Synchrotron, F-38043 Grenoble 9, France

[3] CNRS, LAMS, UMR 8220, F-75005 Paris, France

来源：

VIBRATIONAL SPECTROSCOPY | 2015年 / 80卷

关键词：

beta-amyloid peptide; Surface wettability; Conformational changes; Synchrotron radiation; micro-FTIR; SUPERHYDROPHOBIC SURFACES; FIBRILS; AGGREGATION; SCATTERING; RADIATION; PEPTIDES; PROTEINS; CURCUMIN; FLOW;

D O I：

10.1016/j.vibspec.2015.07.004

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

Here we propose a method to monitor and investigate conformational changes of peptides of high biomedical interest on conventional and nanostructured surfaces by synchrotron infrared micro-spectroscopy. The presence of surfaces with different wettability and the influence of external agents such as acetylcholinesterase and curcumin resulted in marked secondary structure variations of several amyloid-beta fragments (namely A beta(12-28), A beta(25-35), A beta(1-40), A beta(1-42)). The platform could represent a useful tool for the investigation of early stage structural modifications of peptides involved in pathologies of different kind. (C) 2015 Elsevier B.V. All rights reserved.

引用

页码：30 / 35

页数：6

共 25 条

[11] Acetylcholinesterase accelerates assembly of amyloid-beta-peptides into Alzheimer's fibrils: Possible role of the peripheral site of the enzyme [J].