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Can Size Alone Explain Some of the Differences in Toxicity Between β-Amyloid Oligomers and Fibrils? by Ben Keshet; In Hong Yang; Theresa A. Good is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract β‐Amyloid (Aβ) peptide is believed to play a key role in the mechanism of Alzheimer's disease (AD). Aβ tends to aggregate to form amyloid fibrils. A variety of evidence indicates that Aβ aggregates are toxic in vitro and in vivo. An early “Aβ hypothesis” postulated that AD was the consequence of neuron death induced by insoluble deposits of large Aβ fibrils. Newer findings indicate that small soluble Aβ oligomers are the neurotoxic species, yet their structure is still unknown. Many researchers have tried to probe the differences in molecular structure between Aβ oligomers, protofibrils, and fibrils that give rise to their unique toxicities, but with limited success. In this report, we examine the hypothesis that differences in the toxicity of different aggregated Aβ species are the result of differences in species concentration and diffusivity. Using a simple mathematical analysis based on the assumption of a diffusion‐limited reaction, we demonstrate that near 10‐fold differences in toxicity between spherical oligomers and fibrils can be explained from size and concentration arguments. While this work does not suggest that Aβ oligomers and fibrils have identical molec

Who reads Can Size Alone Explain Some of the Differences in Toxicity Between β-Amyloid Oligomers and Fibrils??

Author

Ben Keshet; In Hong Yang; Theresa A. Good

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley - V C H Verlag GmbbH & Co.; Wiley (ISSN 0006-3592)

Published

2010

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)