QSAR of acetylchol inesterase inhibitors: a reexamination of the role of charge-transfer
Su, C.T.; Lien, E.J.
Research Communications in Chemical Pathology and Pharmacology 29(3): 403-415
1980
ISSN/ISBN: 0034-5164 PMID: 7423020 Document Number: 155306
The binding of acetylcholinesterase (AChE) inhibitors to the enzyme is well correlated with substituent constants like logMR, epsilon pi, epsilon sigma, mu, D for series of aromatic methylcarbamates and aromatics. From a correlation study, it appears that charge-transfer effects can be quantitatively separated into steric, electronic and indicator variables (the number of lone pair electrons). Therefore, the interaction of AChE inhibitors with the enzyme can be attributed to the summation of various intermolecular forces as well as to charge-transfer and hydrophobic interactions alone.