Lashuel Hilal A, Grillo-Bosch Dolors
Center for Neurologic Diseases, Brigham and Women's Hospital and Department of Neurology, Harvard Medical School, Boston, MA, USA.
Methods Mol Biol. 2005;299:19-33. doi: 10.1385/1-59259-874-9:019.
Elucidating the structural properties of early intermediates (protofibrils) on the fibril formation pathway of Abeta and alpha-synuclein, the structural relationship among the different intermediates and their relationship to the structure of the amyloid fibrils is critical for understanding the roles of amyloid fibril formation in the pathogenesis of Alzheimer's and Parkinson's diseases. In this chapter we discuss several methods, developed by different laboratories, that enable the preparation and stabilization of amyloid-beta and alpha-synuclein protofibrillar species of defined morphologies for biochemical, biophysical and toxicity studies.
阐明β-淀粉样蛋白（Aβ）和α-突触核蛋白在纤维形成途径中早期中间体（原纤维）的结构特性、不同中间体之间的结构关系以及它们与淀粉样纤维结构的关系，对于理解淀粉样纤维形成在阿尔茨海默病和帕金森病发病机制中的作用至关重要。在本章中，我们将讨论不同实验室开发的几种方法，这些方法能够制备和稳定具有特定形态的β-淀粉样蛋白和α-突触核蛋白原纤维物种，用于生化、生物物理和毒性研究。
