Preparation, anticholinesterase activity and molecular docking of new lupane derivatives
María Julia Castro1, Victoria Richmond2, Carmen Romero3
1INQUISUR-CONICET, Departamento de Química, Universidad Nacional del Sur, Av. Alem 1253, B8000CPB Bahía Blanca, Argentina.
Abstract:
A set of twenty one lupane derivatives (2-22) was prepared from the natural triterpenoid calenduladiol (1) by transformations on the hydroxyl groups at C-3 and C-16, and also on the isopropenyl moiety. The derivatives were tested for their inhibitory activity against acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) and some structure-activity relationships were outlined with the aid of enzyme kinetic studies and docking modelization. The most active compound resulted to be 3,16,30-trioxolup-20(29)-ene (22), with an IC50 value of 21.5μM for butyrylcholinesterase, which revealed a selective inhibitor profile towards this enzyme.
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