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Design, synthesis, and biological evaluation of new territrem B analogues. 2005
Xiangrui Jiang, and
Lei Ao, and
Changxin Zhou, and
Leixiang Yang, and
Qijun Zhang, and
Haibo Li, and
Lianli Sun, and
Xiumei Wu, and
Hua Bai, and
Yu Zhao
Department of Traditional Chinese Medicine and Natural Drug Research, College of Pharmaceutical Sciences, Zhejiang University, Hangzhou 310031, PR China.
Some 23 analogues of the potent acetylcholinesterase (AChE) inhibitor territrem B (1) were designed, synthesized, and tested for their biological activities. Some of the new synthetic derivatives exhibited IC50 values for AChE inhibition in the upper micromolar range. Molecular-modeling studies indicated that a planar conformation seems to be crucial for AChE inhibition. The two N-atoms of the piperazine moieties in 5o, 5p, and 5r might further enhance the inhibitory effects. The cytotoxicities of selected compounds against six human tumor cell lines were also determined.
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