1H nuclear magnetic resonance relaxation investigation of huperzine E binding to acetylcholinesterase

DU Weihong1, LI Yiming2, JIANG Shanhao2, TAN Changheng2, ZHU Dayuan2, GAN Qiuling3

Front. Chem. China ›› 2007, Vol. 2 ›› Issue (4) : 337-342.

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PDF(534 KB)
Front. Chem. China ›› 2007, Vol. 2 ›› Issue (4) : 337-342. DOI: 10.1007/s11458-007-0064-y

1H nuclear magnetic resonance relaxation investigation of huperzine E binding to acetylcholinesterase

  • DU Weihong1, LI Yiming2, JIANG Shanhao2, TAN Changheng2, ZHU Dayuan2, GAN Qiuling3
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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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DU Weihong, LI Yiming, JIANG Shanhao, TAN Changheng, ZHU Dayuan, GAN Qiuling. 1H nuclear magnetic resonance relaxation investigation of huperzine E binding to acetylcholinesterase. Front. Chem. China, 2007, 2(4): 337‒342 https://doi.org/10.1007/s11458-007-0064-y
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