2018年7月23日
Structure-activity relationship of clovamide and its related compounds for the inhibition of amyloid β aggregation
Bioorganic & medicinal chemistry
- ,
- ,
- 巻
- 26
- 号
- 12
- 開始ページ
- 3202
- 終了ページ
- 3209
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.bmc.2018.04.044
- 出版者・発行元
- PERGAMON-ELSEVIER SCIENCE LTD
Alzheimer's disease (AD), a neurodegenerative disorder, is characterized by aggregation of amyloid β-protein (Aβ). Aβ aggregates through β-sheet formation and induces cytotoxicity against neuronal cells. Inhibition of Aβ aggregation by naturally occurring compounds is thus a promising strategy for the treatment of AD. We have already reported that caffeoylquinic acids and phenylethanoid glycosides, which possess two or more catechol moieties, strongly inhibited Aβ aggregation. Clovamide (1) containing two catechol moieties, isolated from cacao beans (Theobroma cacao L.), is believed to exhibit preventive effects on Aβ aggregation. To investigate the structure-activity relationship of clovamide (1) for the inhibition of Aβ aggregation, we synthesized 1 and related compounds 2-11 through reaction between l-DOPA, d-DOPA, l-tyrosine, or l-phenylalanine and caffeic acid, p-coumaric acid, or cinnamic acid, and compounds 12 and 13 were derived from 1. Among tested compounds 1-13, those containing one or two catechol moieties exhibited potent anti-aggregation activity, whereas the non-catechol-type related compounds showed little or no activity. This suggests that at least one cate
- ID情報
-
- DOI : 10.1016/j.bmc.2018.04.044
- ISSN : 1464-3391
- ISSN : 0968-0896
- SCOPUS ID : 85046155028