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Molecular Docking Study on Galantamine Derivatives as Cholinesterase Inhibitors
Author(s) -
Atanasova Mariyana,
Yordanov Nikola,
Dimitrov Ivan,
Berkov Strahil,
Doytchinova Irini
Publication year - 2015
Publication title -
molecular informatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.481
H-Index - 68
eISSN - 1868-1751
pISSN - 1868-1743
DOI - 10.1002/minf.201400145
Subject(s) - galantamine , docking (animal) , acetylcholinesterase , chemistry , stereochemistry , aché , cholinesterase , computational chemistry , pharmacology , donepezil , biochemistry , enzyme , biology , medicine , dementia , nursing , disease , pathology
A training set of 22 synthetic galantamine derivatives binding to acetylcholinesterase was docked by GOLD and the protocol was optimized in terms of scoring function, rigidity/flexibility of the binding site, presence/absence of a water molecule inside and radius of the binding site. A moderate correlation was found between the affinities of compounds expressed as p IC 50 values and their docking scores. The optimized docking protocol was validated by an external test set of 11 natural galantamine derivatives and the correlation coefficient between the docking scores and the p IC 50 values was 0.800. The derived relationship was used to analyze the interactions between galantamine derivatives and AChE.