Delfini M, Gianferri R, Dubbini V, Manetti C, Gaggelli E, Valensin G
Department of Chemistry, University of Rome La Sapienza, P.le A.Moro, Rome, Italy.
J Magn Reson. 2000 May;144(1):129-33. doi: 10.1006/jmre.2000.2031.
Two naphthyridines interacting with Torpedo californica acetylcholinesterase (AChE) were investigated. (1)H NMR spectra were recorded and nonselective, selective, and double-selective spin-lattice relaxation rates were measured. The enhancement of selective relaxation rates could be titrated by different ligand concentrations at constant AChE (yielding 0.22 and 1.53 mM for the dissociation constants) and was providing evidence of a diverse mode of interaction. The double-selective relaxation rates were used to evaluate the motional correlation times of bound ligands at 34.9 and 36.5 ns at 300 K. Selective relaxation rates of bound inhibitors could be interpreted also in terms of dipole-dipole interactions with protons in the enzyme active site.
研究了两种与加州电鳐乙酰胆碱酯酶（AChE）相互作用的萘啶。记录了（1）H NMR谱，并测量了非选择性、选择性和双选择性自旋晶格弛豫率。在恒定的AChE条件下，不同配体浓度可滴定选择性弛豫率的增强（解离常数分别为0.22和1.53 mM），这提供了多种相互作用模式的证据。双选择性弛豫率用于评估300 K时结合配体的运动相关时间，分别为34.9和36.5 ns。结合抑制剂的选择性弛豫率也可以用与酶活性位点中质子的偶极-偶极相互作用来解释。
