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1H nuclear magnetic resonance relaxation investigation of huperzine E binding to acetylcholinesterase |
| DU Weihong1, LI Yiming2, JIANG Shanhao2, TAN Changheng2, ZHU Dayuan2, GAN Qiuling3 |
| 1.Department of Chemistry, Renmin University of China, Beijing 100872, China; Department of Chemistry, Beijing Normal University, Beijing 100875, China; 2.Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China; 3.Department of Chemistry, Beijing Normal University, Beijing 100875, China; |
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Abstract In order to search for better acetylcholinesterase (AchE) inhibitors, the binding properties of AchE with huperizine E, which is a derivative of huperzine A, were investigated with 1H nuclear magnetic resonance (1H NMR) method. The nonselective, selective and double-selective spin-lattice relaxation rates of some protons in huperzine E were acquired in the absence and presence of AchE at a concentration ratio of [ligand]/[protein] = 1 : 0.005. The enhancements of selective relaxation rates of these protons were obvious after adding AchE. The molecular motional correlation times of two pairs of protons, H-1a/H-1b and H-2/H-3, in the bound state at T = 298 K were 11.7 and 9.46 ns respectively, while they were 27.7 and 35.2 ps in the free state. All of these show that huperzine E has high binding affinity with AchE.
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Issue Date: 05 December 2007
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