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基于7-异戊二烯色氨酸合成酶催化合成C-7异戊烯化的吲哚二酮哌嗪生物碱
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引用本文:刘 瑞,张弘弛,李 慧,周 凤.基于7-异戊二烯色氨酸合成酶催化合成C-7异戊烯化的吲哚二酮哌嗪生物碱[J].西北农业学报,2021,(3):413~421
DOI:10.7606/j.issn.1004-1389.2021.03.010
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作者单位
刘 瑞,张弘弛,李 慧,周 凤 (山西大同大学 生命科学学院山西大同 037009山西大同大学 应用生物技术研究所山西大同 037009) 
基金项目:山西省应用基础研究计划(201801D221240);山西省高等学校科技创新项目(2020L0485)。
中文摘要:以L-色氨酸系的二酮哌嗪为底物,7-异戊二烯色氨酸合成酶催化合成异戊烯化的吲哚二酮哌嗪;采用分子对接方法分析底物与酶的亲和关系;采用MTT法测定合成的异戊烯化吲哚二酮哌嗪对3种肿瘤细胞的抑制活性;单因素法优化活性最高的异戊烯化吲哚二酮哌嗪的酶催化条件。结果表明,催化合成7个C-7异戊烯化的吲哚二酮哌嗪生物碱,分子对接结果验证酶催化效率;体外抗肿瘤活性筛选出cyclo-L-7-dimethylallyl-Trp-L-Pro的活性最高,其最佳酶催化条件为:反应时间18 h,温度为35 ℃,pH为8.0(Tris-HCl缓冲液),添加5 mmol·L-1的MgCl2
中文关键词:吲哚二酮哌嗪  7-异戊二烯色氨酸合成酶  分子对接  抗肿瘤活性
 
C-7 Prenylation of Indole Diketopiperazine Alkaloids by 7-dimethylallyl Tryptophan Synthase
Abstract:Catalyzed by 7-dimethylallyl tryptophan synthetase,the the prenylated indole diketopiperazines was synthesized bycyclic dipeptides containing L-tryptophan,the molecular docking method was used to analyze the affinity between the substrate and the enzym and the MTT method was used to determine the inhibitory activity of the synthesized prenylated indole diketopiperazines on three kinds of tumor cells;enzymatic catalytic conditions of the most active synthetic product were optimized by the single factor method. The results showed that seven C-7 prenylated indolepiperazines were synthesize,the enzyme catalytic efficiency was also verified by the results of molecular docking; cyclo-L-7-dimethylallyl-Trp-L-Pro screened with In vitro anti-tumor activity showed the highest activity,which the optimal enzymatic conditions were reaction time of 18 h,temperature of 35 ℃,pH 8.0(Tris-HCl buffer),and 5 mmol·L-1 MgCl2.
keywords:Indole diketopiperazine  7-Dimethylallyl tryptophan synthase  Molecular docking  Antitumor activity
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