Book Chapters
Permanent URI for this collection
Browse
Browsing Book Chapters by Author "Edwin, Nadia J."
Now showing 1 - 3 of 3
Results Per Page
Sort Options
Item Elucidating the Kinetics of β-amyloid Fibril Formation(American Chemical Society, 2005) Edwin, Nadia J.The formation of β-Amyloid peptide (Aβ1-40) aggregates was monitored by dynamic light scattering. Various sizes of materials may be present throughout the aggregation process, but small scatterers are difficult to detect in the presence of large ones. Fluorescence photobleaching recovery studies on 5-carboxyfluorescein-labeled Aβ1-40 peptide solutions readily confirmed the presence of large and small species simultaneously. The effects of dye substitution on the aggregation behavior of Aβ1-40 peptide are subtle, but should not prevent further investigations by fluorescence photobleaching recovery or other fluorescence methods.Item Fluorescence Photobleaching Recovery: A Primer(Springer, 2008) Edwin, Nadia J.Item β-amyloid Protein Aggregation(Humana Press, 2007) Edwin, Nadia J.The β-amyloid peptide aggregates via a nucleation pathway where micellar aggregates propagate to form oligomers (protofibrils), which then polymerize into insoluble fibrils. This fibrillogenic process has been linked to the pathogenesis associated with Alzheimer’s disease. One purpose of this chapter is to provide a protocol for reliably producing monomeric Aβas a starting point for physical and biological studies. Many research groups have used organic solvents to disaggregate pre-seeded Aβ in an attempt to acquire monomeric starting materials. Others have used instrumental techniques such as size exclusion chromatography to isolate monomer, structural intermediates, and fibrils and study their affects on A β nucleation. This chapter discusses a modified method of A βpreparation using organic solvents followed by dissolution into aqueous phosphate buffer systems that renders monomeric A β starting solutions for kinetic experiments. Additionally, this chapter details a number of physical techniques such as scanning force microscopy, circular dichroism spectroscopy, transmission electron microscopy, fluorescence spectroscopy, fluorescence photobleaching recovery, and dynamic light scattering, together with physiological techniques such as cell viability assays to characterize Aβ nucleation, aggregation, and fibrillization and the potential biological activity of the various A βparticles.