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CH/π hydrogen bonds as evidenced in the substrate specificity of acetylcholine esterase
Author(s) -
Umezawa Yoji,
Nishio Motohiro
Publication year - 2005
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20352
Subject(s) - chemistry , hydrogen bond , acetylcholine , preprint , aché , cholinesterase , acetylcholinesterase , esterase , substrate (aquarium) , torpedo , stereochemistry , enzyme , biochemistry , molecule , pharmacology , acetylcholine receptor , organic chemistry , computer science , world wide web , medicine , oceanography , receptor , geology
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/π 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. © 2005 Wiley Periodicals, Inc. Biopolymers 79: 248–258, 2005 This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com