1H NMR relaxation investigation of acetylcholinesterase inhibitors from huperzine A and derivative.
The binding properties of huperzine A (1) with Torpediniforms Nacline acetylcholinesterase (TnAChE) were investigated by (1)H NMR methods. The noselective, selective and double-selective spin-lattice relaxation rates were acquired in absent and present of TnAChE at a ratio [ligand]/[protein]=1:0.005. The selective relaxation rates shown protons of 1 had dipole-dipole interaction with protein active site protons. The motional correlation time of bound ligand was calculated by double-selective relaxation rate at 1 tau(2,3)=40.5 ns at 298 K, which showed 1 had high affinity with TnAChE. The experiments give a possible method to use TnAChE to locate the new huperzine A derivatives as AChE inhibitors.
Li
Yiming
Y
State Key Laboratory for Drug Research, Shanghai Institute of Materia Medica, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, 555 Zuchongzhi Road, Shanghai 201203, China.
Li
Qian
Q
Sun
Manchi
M
Song
Guoqiang
G
Jiang
Shanhao
S
Zhu
Dayuan
D
D000470:Alkaloids; D000818:Animals; D002800:Cholinesterase Inhibitors / Q000302:isolation & purification* / Q000494:pharmacology; D032501:Huperzia; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D012717:Sesquiterpenes / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D014101:Torpedo
D000470:Alkaloids; D002800:Cholinesterase Inhibitors; D012717:Sesquiterpenes; C050426:huperzine A; D006859:Hydrogen