Pansieri Jonathan, Halim Mohammad A, Vendrely Charlotte, Dumoulin Mireille, Legrand François, Sallanon Marcelle Moulin, Chierici Sabine, Denti Simona, Dagany Xavier, Dugourd Philippe, Marquette Christel, Antoine Rodolphe, Forge Vincent
Univ. Grenoble Alpes , CNRS , CEA , BIG/CBM/AFFOND , F-38000 Grenoble , France . Email:
Institut Lumière Matière , UMR 5306 , Université Claude Bernard Lyon 1 , CNRS , F-69622 Lyon , France . Email:
Chem Sci. 2018 Feb 5;9(10):2791-2796. doi: 10.1039/c7sc04542e. eCollection 2018 Mar 14.
Heterogeneity and polymorphism are generic features of amyloid fibers with some important effects on the related disease development. We report here the characterization, by charge detection mass spectrometry, of amyloid fibers made of three polypeptides involved in neurodegenerative diseases: Aβ peptide, tau and α-synuclein. Beside the mass of individual fibers, this technique enables to characterize the heterogeneity and the polymorphism of the population. In the case of Aβ peptide and tau protein, several coexisting species could be distinguished and characterized. In the case of α-synuclein, we show how the polymorphism affects the mass and charge distributions.
异质性和多态性是淀粉样纤维的普遍特征,对相关疾病的发展有一些重要影响。我们在此报告通过电荷检测质谱对由三种与神经退行性疾病相关的多肽(β-淀粉样肽、tau蛋白和α-突触核蛋白)构成的淀粉样纤维的表征。除了单个纤维的质量外,该技术还能够表征群体的异质性和多态性。对于β-淀粉样肽和tau蛋白,可以区分和表征几种共存的物种。对于α-突触核蛋白,我们展示了多态性如何影响质量和电荷分布。