A New Method to Measure Cellular Toxicity of Non-Fibrillar and Fibrillar Alzheimer's Aβ Using Yeast

Article type: Short Communication

Authors: Bharadwaj, Prashant^{a; b} | Waddington, Lynne^a | Varghese, Jose^a | Macreadie, Ian G.^{a; *}

Affiliations: [a] CSIRO Molecular and Health Technologies and P-Health Flagship, Parkville, VIC, Australia | [b] Royal Melbourne Institute of Technology, Bundoora, Australia

Correspondence: [*] Corresponding author. CSIRO Molecular and Health Technologies, 343 Royal Parade, Parkville, Victoria 3052, Australia. Tel.: +61 3 9662 7299; Fax: +61 3 9662 7266; E-mail: ian.macreadie@csiro.au.

Abstract: The 42 amino acid amyloid-β (Aβ) can exist in multiple physical states including oligomers and fibrils. This study shows that fibril formation is hastened by the biological buffers required to support the growth of mammalian cells, but is prevented if Aβ is maintained in water. Here we describe a method to produce Aβ in oligomeric form and the comparison of stable fibrillar and non-fibrillar forms in cell toxicity studies in water, achieved through the use of yeast. We show that extracellular, non-fibrillar Aβ causes a dose dependent loss of cell viability while fibrillar Aβ has low toxicity.

DOI: 10.3233/JAD-2008-13204

Journal: Journal of Alzheimer's Disease, vol. 13, no. 2, pp. 147-150, 2008