New Acylate and Thioacylate Effectors of Mammalian Cholinesterases Based on Cyclic Ammonium Alcohols Containing Elements of the Anabasine Structure


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Abstract

We report a pioneering analysis of the interaction between mammalian cholinesterases and 36 acylates and thioacylates of ammonium alcohols with different structure of an alkyl chain between ammonium and etheric atoms and with different structure of a cyclic ammonium group. Among these ethers, which were both substrates and reversible inhibitors of erythrocyte cholinesterase and serum butyrylcholinesterase, specific effectors of both enzymes were identified.

About the authors

N. E. Basova

Sechenov Institute of Evolutionary Physiology and Biochemistry

Author for correspondence.
Email: basovn@rambler.ru
Russian Federation, St. Petersburg

B. N. Kormilitsyn

Sechenov Institute of Evolutionary Physiology and Biochemistry

Email: basovn@rambler.ru
Russian Federation, St. Petersburg

A. Yu. Perchenok

Sechenov Institute of Evolutionary Physiology and Biochemistry

Email: basovn@rambler.ru
Russian Federation, St. Petersburg

E. V. Rozengart

Sechenov Institute of Evolutionary Physiology and Biochemistry

Email: basovn@rambler.ru
Russian Federation, St. Petersburg

V. S. Saakov

Sechenov Institute of Evolutionary Physiology and Biochemistry

Email: basovn@rambler.ru
Russian Federation, St. Petersburg

A. A. Suvorov

Sechenov Institute of Evolutionary Physiology and Biochemistry

Email: basovn@rambler.ru
Russian Federation, St. Petersburg

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