Author： Zheng Zhi-Hui Dong Yue-Sheng Zhang Hua Lu Xin-Hua Ren Xiao Zhao Guiyu He Jian-Gong Si Shu-Yi
Publisher： Informa Healthcare
ISSN： 1475-6366
Source： Journal of Enzyme Inhibition and Medicinal Chemistry, Vol.22, Iss.1, 2007-02, pp. : 43-49
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Abstract
A high throughput screening was carried out in order to search for inhibitors of acetylcholinesterase (AChE) from microorganism metabolites. An actinomycete strain was found to produce active compounds named N98-1272 A, B and C with IC50 of 15.0, 11.5, 12.5 μM, respectively. Structural studies revealed that the three compounds are identical to the known antibiotics, Manumycin C, B and A. Kinetic analyses showed that N98-1272 C (Manumycin A) acted as a reversible noncompetitive inhibitor of acetylcholinesterase, with a Ki value of 7.2 μM. The cyclohexenone epoxide part of the structure plays a crucial role in the inhibitory activity against AChE. Compared with Tacrine, N98-1272 A, B, and C exhibit much better selectivity toward AChE over BuChE.
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