Regulation of in vitro Aβ1-40 Aggregation Mediated by Small Molecules

Title
Regulation of in vitro Aβ1-40 Aggregation Mediated by Small Molecules
Authors
김혜연김영수한균희김동진
Keywords
아밀로이드; amyloid; 알츠하이머; alzheimer; 치매; 신약; 소분자; Alzheimer's disease; amyloid-β; fibril
Issue Date
2010-10
Publisher
Journal of Alzheimers disease
Citation
VOL 22, NO 1, 73-85
Abstract
It is well known that the transient and prolonged misfolding nature of amyloid β (Aβ) makes it difficult to perform proper in vitro studies and obtain consistent results. From monomers to fibrils, the aggregated forms of Aβ are significant hallmarks in the Alzheimer’s disease (AD) cascade and become the valuable targets for early diagnosis and therapy for AD. Thus, development of optimized in vitro fibrillogenic conditions to induce the desired Aβ states is essential to AD research. In this study, fifteen organic amino acid compounds (glycine, taurine, tramiprosate, and their derivatives) were employed to induce different fibrillogenic conditions for Aβ. The fibrillogenic patterns of Aβ peptides in these compounds were analyzed by thioflavin T assay and SDSPAGE with photoinduced crosslinking of unmodified proteins protocols, then were analyzed and compared to those obtained via transmission electron microscopy and neuronal cell viability assays. Our study suggests various compounds capable of inducing different levels of in vitro Aβ1−40 fibrillogenesis, potentially useful tools in the study of Aβ for AD.
URI
http://pubs.kist.re.kr/handle/201004/38599
ISSN
1387-2877
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KIST Publication > Article
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