The conformational aspects of the interaction of the cholinesterases of Pacific Ocean squid and vertebrates with derivatives of polymethylene bis(trimethylammonium).

Conformational properties of a series of polymethylenebis (trimethylammonium) derivatives [formula: see text] (n = 4-10), cholinesterase reversible inhibitors, were studied by molecular mechanics method. Conformation-activity relationships between these inhibitors and human erythrocyte acetylcholinesterase, horse plasma butyrylcholinesterase, cholinesterases from the brain of the frog Rana temporaria and from visual ganglia of the squid Todarodes pacificus were investigated by correlational methods. Differences in mechanisms of antienzyme actions were determined.