In-silico identification of the binding mode of synthesized adamantyl derivatives inside cholinesterase enzymes.

ABSTRACT:

Aim

To investigate the binding mode of synthesized adamantly derivatives inside of cholinesterase enzymes using molecular docking simulations.

Methods

A series of hybrid compounds containing adamantane and hydrazide moieties was designed and synthesized. Their inhibitory activities against acetylcholinesterase (AChE) and (butyrylcholinesterase) BChE were assessed in vitro. The binding mode of the compounds inside cholinesterase enzymes was investigated using Surflex-Dock package of Sybyl7.3 software.

Results

A total of 26 adamantyl derivatives were synthesized. Among them, adamantane-1-carboxylic acid hydrazide had an almost equal inhibitory activity towards both enzymes, whereas 10 other compounds exhibited moderate inhibitory activity against BChE. The molecular doc

SUBMITTER: Al-Aboudi A 

PROVIDER: S-EPMC4648121 | biostudies-literature | 2015 Jul

REPOSITORIES: biostudies-literature