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In Vitro Preparation of Prefibrillar Intermediates of Amyloid-β and α Synuclein

  • Hilal A. Lashuel
  • Dolors Grillo-Bosch
Part of the Methods in Molecular Biology™ book series (MIMB, volume 299)

Abstract

Elucidating the structural properties of early intermediates (protofibrils) on the fibril formation pathway of Aβ and α-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-β and α-synuclein protofibrillar species of defined morphologies for biochemical, biophysical and toxicity studies.

Key Words

Alzheimer's disease (AD) Parkinson's disease (PD) amyloid fibrils protofibrils oligomers amyloid-β(Aβ) derived diffusible ligand (ADDLS) amylospheriods annular structures pores size exclusion chromatography (SEC) electron microscopy (EM) atomic force microscopy (AFM) analytical ultracentrifugation (AU) scanning transmission electron microscopy (STEM) arctic variant (E22G) wild-type (WT). 

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Copyright information

© Humana Press Inc. 2005

Authors and Affiliations

  • Hilal A. Lashuel
    • 1
  • Dolors Grillo-Bosch
    • 2
  1. 1.Center for Neurologic Diseases, Brigham and Women's Hospital and Department of NeurologyHarvard Medical SchoolCambridge
  2. 2.Departament de Quimica OrganicaUniversitat de BarcelonaBarcelonaSpain

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