QSAR OF ACETYLCHOLINESTERASE INHIBITORS - A REEXAMINATION OF THE ROLE OF CHARGE-TRANSFER

  • 1 January 1980
    • journal article
    • research article
    • Vol. 29  (3) , 403-415
Abstract
The binding of acetylcholinesterase (AChE) inhibitors to the enzyme is well correlated with substituent constants like logMR [molar refraction], .SIGMA..pi. [log of the octanol-water partition coefficient], .SIGMA..sigma. [Hammett''s sigma constant], .mu. [dipole moment of the polar moiety], D [available number of lone pair electrons from N and O atoms] for series of aromatic methylcarbamates and aromatics. A correlation study suggests that charge-transfer effects can be quantitatively separated into steric, electronic and indicator variables (the number of lone pair electrons). The interaction of AChE inhibitors with the enzyme can be attributed to the summation of various intermolecular forces and to charge-transfer and hydrophobic interactions alone.