The principal histopathological feature of Alzheimer's disease is the presence of beta-amyloid (Abeta) aggregates in the brain, and researchers believe that various environmental factors play significant roles in the conformational change of Abeta. Therefore, discovering a rapid and convenient analytical method of evaluating the environmental factors on Abeta aggregation would have a considerable impact. Herein we report our development of a novel microfluidic screening system enabling high-throughput analysis, low-consumption of reagents, and short analytical time. In this work, we investigated (1) the temporal evolution of Abeta aggregation within microchannels and (2) the high-throughput screening of the inhibitory effect of small molecules and metal ions against Abeta aggregation by using ThT-induced fluorescence microscopy and ex situ atomic force microscopy. The microfluidic system should contribute to a simultaneous analysis of multiple environmental factors affecting amyloid aggregates in a parallel manner and to screen therapeutic small molecules prior to their in vivo evaluation.Our Recent Publications Related to This Presentation:J. S. Lee, J. Ryu, C. B. Park. Analytical Chemistry 81:2751-2759 (2009).J. S. Lee, E. Um, J-K. Park, C. B. Park. Langmuir 24:7068-7071 (2008).

High-throughput analysis of Alzheimer's β-amyloid aggregation using microfluidic self-assembly

239th National Meeting (2010)

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