https://scholars.lib.ntu.edu.tw/handle/123456789/406778
Title: | Development of a novel diffusion-based method to estimate the size of the aggregated A£] species responsible for neurotoxicity | Authors: | Wang S.S.-S. Becerra-Arteaga A. Good T.A. |
Keywords: | Alzheimer's disease;A£];Diffusion;Diffusion coefficient;Molecular weight;Neurotoxicity | Issue Date: | 2002 | Journal Volume: | 80 | Journal Issue: | 1 | Start page/Pages: | 50-59 | Source: | Biotechnology and Bioengineering | Abstract: | £]-Amyloid peptide (A£]) is the primary protein component of senile plaques in Alzheimer's disease and is believed to be responsible for the neurodegeneration associated with the disease. A£] is toxic only when aggregated, however, the size and structure of the aggregated species associated with toxicity is unknown. In the present study, we developed a diffusion-based method to simultaneously separate and detect the biological activity of toxic A£] oligomers and used the method to examine the relationship between size of aggregated protein and toxicity to SH-SY5Y cells. From these measurements, the effective diffusivity and hydrodynamic radius of the toxic oligomeric species of A£] could be determined. A sensitivity analysis was performed to examine the effects of model assumptions used in data analysis on the effective diffusivity calculated. The method provides a new estimate of the size of small toxic A£] species associated with fibril formation. This work contributes to our understanding of the relationship between A£] structure and toxicity and with further refinements may aid in our ability to design agents which alter the A£] aggregation/dissociation processes associated with neurotoxicity. ? 2002 Wiley Periodicals, Inc. |
URI: | https://scholars.lib.ntu.edu.tw/handle/123456789/406778 | ISSN: | 00063592 | DOI: | 10.1002/bit.10347 |
Appears in Collections: | 化學工程學系 |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.