M. Delfini et al., H-1 NMR relaxation investigation of inhibitors interacting with Torpedo californica acetylcholinesterase, J MAGN RES, 144(1), 2000, pp. 129-133
Two naphthyridines interacting with Torpedo californica acetylcholinesteras
e (AChE) were investigated. H-1 NMR spectra were recorded and nonselective,
selective, and double-selective spin-lattice relaxation rates were measure
d. The enhancement of selective relaxation rates could be titrated by diffe
rent 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 t
he motional correlation times of bound ligands at 34.9 and 36.5 us 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 si
te, (C) 2000 Academic Press.