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毛细管电泳分析单体 Abeta(1-40)肽。

Analysis of monomeric Abeta (1-40) peptide by capillary electrophoresis.

机构信息

Department of Chemistry, Louisiana State University, Baton Rouge, LA 70803, USA.

出版信息

Analyst. 2010 Jul;135(7):1631-5. doi: 10.1039/c0an00080a. Epub 2010 May 6.

Abstract

A method was developed to characterize and quantify preparations of monomeric beta-amyloid (Abeta) peptide using capillary electrophoresis (CE) with UV absorbance detection. The detection limit for Abeta monomer using this method was 0.5 microM (19 pg). The self-assembly of Abeta to form amyloid fibrils is closely linked to Alzheimer's disease and is the subject of intense investigations. Consistent preparation of Abeta monomer samples at known concentrations and free of aggregates is a significant challenge for researchers studying the mechanism of Abeta fibril formation and searching for small molecules that inhibit Abeta fibril formation. Samples of Abeta monomer are known to sometimes contain pre-existing aggregates that can affect the kinetics and structure of amyloid fibrils. The CE method presented here showed that some of the monomeric Abeta samples prepared for this study contained a species producing a second peak (in addition to the major monomer peak). The aggregation was monitored using a thioflavin T fluorescence assay, and the resulting fibrils were characterized by transmission electron microscopy. Monomer samples containing the additional peak based on CE analysis were shown to aggregate more rapidly than monomer samples that were free of this putative Abeta aggregate peak.

摘要

开发了一种使用毛细管电泳(CE)结合紫外吸收检测来对单体β-淀粉样蛋白(Abeta)肽进行特征描述和定量的方法。使用该方法检测 Abeta 单体的检测限为 0.5 microM(19 pg)。Abeta 的自组装形成淀粉样纤维与阿尔茨海默病密切相关,是研究的热点。对于研究 Abeta 纤维形成机制并寻找抑制 Abeta 纤维形成的小分子的研究人员来说,以已知浓度且无聚集物的方式一致地制备 Abeta 单体样品是一项重大挑战。已知 Abeta 单体样品有时会包含预先存在的聚集物,这可能会影响淀粉样纤维的动力学和结构。本文提出的 CE 方法表明,本研究中制备的一些 Abeta 单体样品中存在产生第二个峰(除主要单体峰之外)的物质。使用硫黄素 T 荧光测定法监测聚集,并用透射电子显微镜对所得纤维进行了表征。根据 CE 分析含有附加峰的单体样品显示比没有这种假定的 Abeta 聚集物峰的单体样品更快地聚集。

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