High-Throughput Analysis of Alzheimer's beta-Amyloid Aggregation Using a Microfluidic Self-Assembly of Monomersf

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dc.contributor.authorLee, Joon Seokko
dc.contributor.authorRyu, Jungkiko
dc.contributor.authorPark, Chan Beumko
dc.date.accessioned2009-06-15T09:47:39Z-
dc.date.available2009-06-15T09:47:39Z-
dc.date.created2012-02-06-
dc.date.created2012-02-06-
dc.date.issued2009-04-
dc.identifier.citationANALYTICAL CHEMISTRY, v.81, no.7, pp.2751 - 2759-
dc.identifier.issn0003-2700-
dc.identifier.urihttp://hdl.handle.net/10203/9432-
dc.description.abstractThe principal histopathological feature of Alzheimer's disease is the presence of beta-amyloid (A beta) aggregates in the gray matter of the brain, and researchers believe that various environmental factors play significant roles in the conformational change and self-assembly of A beta peptides. Therefore, discovering a rapid and convenient analytical method of evaluating the environmental factors on A beta 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. Microchannels with a cross-sectional. dimension of 100 mu m x 100 mu m were immobilized with A beta monomers via N-hydroxysuccinimide ester activation of the internal surfaces, and then a fresh A beta monomer solution mixed with different small molecules or metal ions was continuously introduced into the microchannels to induce A beta aggregation. In this work, we investigated (1) the temporal evolution of A beta aggregation within microchannels, (2) the high-throughput screening of the inhibitory effect of 12 small molecules against A beta aggregation, and (3) the effect of different metal ions (Fe(3+), Cu(2+), Zn(2+), and Al(3+)) on A beta aggregation by using thioflavin T (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.-
dc.description.sponsorshipThis research was supported by Grants from the BioGreen 21 Program (20070301034038) and the Korea Science and Engineering Foundation (KOSEF) National Research Laboratory (NRL) program (R0A-2008-000-20041-0). This research was also partially supported by a Grant from the Eco-Technopia 21 project (010-081-036) from the Ministry of Environment, Republic of Koreaen
dc.languageEnglish-
dc.language.isoen_USen
dc.publisherAmer Chemical Soc-
dc.subjectFIBRILS IN-VITRO-
dc.subjectSOLID-SURFACE-
dc.subjectPROTEIN AGGREGATION-
dc.subjectMETAL-IONS-
dc.subjectDISEASE-
dc.subjectPEPTIDE-
dc.subjectNEUROTOXICITY-
dc.subjectA-BETA-42-
dc.subjectFIBRILLOGENESIS-
dc.subjectTHERAPEUTICS-
dc.titleHigh-Throughput Analysis of Alzheimer's beta-Amyloid Aggregation Using a Microfluidic Self-Assembly of Monomersf-
dc.typeArticle-
dc.identifier.wosid000264759400045-
dc.identifier.scopusid2-s2.0-64849106509-
dc.type.rimsART-
dc.citation.volume81-
dc.citation.issue7-
dc.citation.beginningpage2751-
dc.citation.endingpage2759-
dc.citation.publicationnameANALYTICAL CHEMISTRY-
dc.identifier.doi10.1021/ac802701z-
dc.embargo.liftdate9999-12-31-
dc.embargo.terms9999-12-31-
dc.contributor.localauthorPark, Chan Beum-
dc.type.journalArticleArticle-
dc.subject.keywordPlusFIBRILS IN-VITRO-
dc.subject.keywordPlusSOLID-SURFACE-
dc.subject.keywordPlusPROTEIN AGGREGATION-
dc.subject.keywordPlusMETAL-IONS-
dc.subject.keywordPlusDISEASE-
dc.subject.keywordPlusPEPTIDE-
dc.subject.keywordPlusNEUROTOXICITY-
dc.subject.keywordPlusA-BETA-42-
dc.subject.keywordPlusFIBRILLOGENESIS-
dc.subject.keywordPlusTHERAPEUTICS-
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