Original scientific paper

https://doi.org/10.5562/cca2060

Binding Modes of Quinuclidinium Esters to Butyrylcholinesterase

Ines Primožič orcid.org/0000-0003-1154-4735 ; Department of Chemistry, Faculty of Science, University of Zagreb, Horvatovac 102A, HR­10 000 Zagreb, Croatia
Tomica Hrenar ; Department of Chemistry, Faculty of Science, University of Zagreb, Horvatovac 102A, HR­10 000 Zagreb, Croatia
Srđanka Tomić ; Department of Chemistry, Faculty of Science, University of Zagreb, Horvatovac 102A, HR­10 000 Zagreb, Croatia

Abstract

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 pat-terns for enantiomers, which define their reactivity. Calculated Gibbs energies of binding obtained by mo-lecular docking simulations were well correlated to the experimentally determined binding affinities of the investigated chiral esters. (doi: 10.5562/cca2060)

Keywords

butyrylcholinesterase; quinuclidinium esters; BChE-ester complexes; docking studies

Hrčak ID:

80416

URI

https://hrcak.srce.hr/80416

Publication date:

30.4.2012.

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