Abstract
The preparation of the choline esters of cis- and trans-4-t-butylcyclohexanecarboxylic acid is reported. The similar inhibitory potency displayed by these isomers towards the acetylcholinesterase catalysed hydrolysis of acetylcholine is explained on the basis of the binding of a thermodynamically unstable conformation of the cis-isomer to the active site. Similar studies employing the β-trimethylammoniopropionate esters of cis- and trans-4-t-butylcyclohexanol suggest that the “reverse esters” do not bind to the active site in an identical manner to the acylcholines.