Springer Protocols: Abstract: In Vitro Preparation of Prefibrillar Intermediates of Amyloid-β and α Synuclein

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

By: Hilal A. Lashuel², Dolors Grillo-Bosch³

Abstract

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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.

Affiliation(s): (2) Center for Neurologic Diseases, Brigham and Women's Hospital and Department of Neurology, Harvard Medical School, Cambridge, MA
(3) Departament de Quimica Organica, Universitat de Barcelona, Barcelona, Spain

Book Title: Amyloid Proteins: Methods and Protocols

Series: Methods in Molecular Biology | Volume: 299 | Pub. Date: Dec-28-2004 | Page Range: 19-33 | DOI: 10.1385/1-59259-874-9:019

Subject: Protein Science

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).

References

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