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.
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.
Yiming
Y
Li
Qian
Q
Li
Manchi
M
Sun
Guoqiang
G
Song
Shanhao
S
Jiang
Dayuan
D
Zhu
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