Studies of Polymorphism of Amyloid-β42 Peptide from Different Suppliers

被引:30
作者
Suvorina, Mariya Yu. [1 ]
Selivanova, Olga M. [1 ]
Grigorashvili, Elizaveta I. [1 ]
Nikulin, Alexey D. [1 ]
Marchenkov, Victor V. [1 ]
Surin, Alexey K. [1 ,2 ]
Galzitskaya, Oxana V. [1 ]
机构
[1] Russian Acad Sci, Inst Prot Res, Pushchino 142290, Moscow Region, Russia
[2] State Res Ctr Appl Microbiol & Biotechnol, Obolensk, Moscow Region, Russia
基金
俄罗斯科学基金会;
关键词
A beta(42) peptide; Alzheimer's disease; amyloid fibril; electron microscopy; mass spectroscopy; oligomer; prion-like behavior; protofibril; ALZHEIMERS-DISEASE; A-BETA; CONCENTRATION-DEPENDENCE; SECONDARY NUCLEATION; ELECTRON-MICROSCOPY; AMYLOID FIBRILS; FOLDING NUCLEI; IN-VITRO; LAG-TIME; PROTEIN;
D O I
10.3233/JAD-150147
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
The aim of this study was to investigate the process of amyloidogenesis of amyloid-beta (A beta)(42) peptide, by means of fluorescence spectroscopy, electron microscopy, X-ray diffraction, and mass spectrometry. It has been repeatedly reported in the literature that the process of fibril formation by A beta(42) peptide depends considerably not only upon the specific conditions (ionic conditions, pH, temperature, mixing, etc.), as well as the manufacturing route (synthetic or recombinant), but also on the methods of synthesis and purification. We have, for the first time, systematically analyzed samples of A beta(42) peptide supplied by five different companies (Anaspec, Invitrogen, Enzo, Sigma-Aldrich, and SynthAssist) and obtained evidence of significant variability, including lot to lot variations. All studied samples formed amyloid-like fibrils at pH3-6, and the fibrils contained cross-beta structures. Samples from Anaspec, Invitrogen, and Enzo formed one particular type of amyloid-like fibrils, while the samples from Sigma-Aldrich and SynthAssist formed another distinct type of fibrils. The observed polymorphism emphasizes the capacity of the A beta(42) peptide to act as a prion agent with varying structural characteristics. The presented data have allowed us to propose a possible mechanism of formation of amyloid-like fibrils.
引用
收藏
页码:583 / 593
页数:11
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