Bioactive aromatic metabolites from the sea urchin-derived actinomycete Streptomyces spectabilis strain HDa1
文献类型： 外文期刊
作者： Guo, Zhi Kai 1 ; Wang, Rong 2 ; Chen, Fu Xiao 2 ; Liu, Tian Mi 3 ; Yang, Ming Qiu 2 ;
作者机构： 1.Chinese Acad Trop Agr Sci, Minist Agr, Inst Trop Biosci & Biotechnol, Key Lab Biol & Genet Resources Trop Crops, Haikou 571101, Hainan, Peoples R China
2.Hainan Acad Ocean & Fisheries Sci, Haikou 570203, Hainan, Peoples R China
3.Hainan Testing Ctr Qual & Safety Aquat Prod, Haikou 570206, Hainan, Peoples R China
关键词： Sea urchin; Actinomycete; Natural product; Acetylcholinesterase inhibitor
期刊名称：PHYTOCHEMISTRY LETTERS （ 影响因子：1.679； 五年影响因子：1.861 ）
ISSN： 1874-3900
年卷期： 2018 年 25 卷
页码：
收录情况： SCI
摘要： An actinomycete strain HDa1, capable of producing new acetylcholinesterase (AchE) inhibitors, was isolated from the gut of sea urchin Anthocidaris crassispina and identified as Streptomyces spectabilis by morphology and 16S rRNA gene sequence. Chemical investigation of the fermentation broth of Streptomyces spectabilis HDa1 by bioactivity-guided fractionation led to the isolation of 3,4-dimethoxy-1-naphthamide (1), p-O-(3,3-dimethylallyl)- benzamide (2), cyclo-(L-Val-L-Pro) (3), cyclo-(L-Ile-L-Pro) (4) and cyclo-(L-Leu-L-Pro) (5). Their structures were determined by analysis of the high-resolution electrospray ionization mass spectrum (HRESIMS), one-dimension (H-1-, C-13 NMR) and two-dimension NMR experiments (HSQC, HMBC and H-1-H-1 COSY), as well as by comparison with those data of known compounds. Compound 1 was identified as a new compound and compound 2 was discovered as a microbial natural product for the first time. All of these isolated compounds were evaluated for acetylcholinesterase inhibitory activity, with compounds 1 and 2 displaying in vitro inhibitory activity against AChE with the inhibition percentage of 54.8% and 43.5%, respectively, at the concentration of 100 mu M. These two natural AChE inhibitors may provide a new chance for drug development for the treatment of neural degeneration disease.
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