|
篇目详细内容 |
【篇名】 |
1H nuclear magnetic resonance relaxation investigation of huperzine E binding to acetylcholinesterase |
【刊名】 |
Frontiers of Chemistry in China |
【刊名缩写】 |
Front. Chem. China |
【ISSN】 |
1673-3495 |
【EISSN】 |
1673-3614 |
【DOI】 |
10.1007/s11458-007-0064-y |
【出版社】 |
Higher Education Press and Springer-Verlag |
【出版年】 |
2007 |
【卷期】 |
2
卷4期 |
【页码】 |
337-342
页,共
6
页 |
【作者】 |
DU Weihong;
LI Yiming;
GAN Qiuling;
JIANG Shanhao;
TAN Changheng;
ZHU Dayuan;
|
【关键词】 |
huperzine E; acetylcholinesterase; proton spinlattice relaxation rate; molecular motional correlation time; nuclear magnetic resonance (NMR) |
【摘要】 |
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. |
|