期刊
CROATICA CHEMICA ACTA
卷 85, 期 1, 页码 77-83出版社
CROATIAN CHEMICAL SOC
DOI: 10.5562/cca2060
关键词
butyrylcholinesterase; quinuclidinium esters; BChE-ester complexes; docking studies
资金
- Croatian Ministry of Science, Education and Sports [119-1191344-3121]
The orientations of chiral quinuclidin-3-ol esters and benzoylcholine in the active site of horse butyrylcholinesterase have been investigated by flexible ligand docking. Change of the esters' acyl moiety as well as the substituent at the quinuclidinium nitrogen atom affected the activity and stereoselectivity of the biotransformations. Analysis of interactions in the active site revealed the most important binding patterns for enantiomers, which define their reactivity. Calculated Gibbs energies of binding obtained by molecular docking simulations were well correlated to the experimentally determined binding affinities of the investigated chiral esters. (doi: 10.5562/cca2060)
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