title: CH/pi hydrogen bonds as evidenced in the substrate specificity of acetylcholine esterase.
abstract: The crystal structure of acetylcholine esterase (AchE) in complex with various inhibitors, investigated as drugs for improvement of the cognitive ability of early stage Alzheimer's disease, has been analyzed with the use of our program CHPI. A number of CH/pi hydrogen bonds have been disclosed in the binding of the inhibitors with Torpedo californica AchE. It has been demonstrated that, in order to be effective in the binding with AchE, C-H bonds in the inhibitor need not be polarized.
authors.affiliation: Microbial Chemistry Research Center, Shinagawa-ku, Tokyo 141-0021, Japan. umezaway@bikaken.or.jp
authors.forename: Yoji
authors.initials: Y
authors.lastname: Umezawa
authors.forename: Motohiro
authors.initials: M
authors.lastname: Nishio
mesh_terms: D000109:Acetylcholine / Q000737:chemistry; D000110:Acetylcholinesterase / Q000737:chemistry*; D000544:Alzheimer Disease / Q000378:metabolism*; D000818:Animals; D001704:Biopolymers / Q000737:chemistry*; D002244:Carbon / Q000737:chemistry; D018360:Crystallography, X-Ray; D004247:DNA / Q000737:chemistry; D019281:Dimerization; D006860:Hydrogen Bonding; D008024:Ligands; D008956:Models, Chemical; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D012984:Software; D013379:Substrate Specificity; D014101:Torpedo / Q000378:metabolism
chemical_list: D001704:Biopolymers; D008024:Ligands; D002244:Carbon; D004247:DNA; D000110:Acetylcholinesterase; D000109:Acetylcholine