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Croatica Chemica Acta, Vol. 85 No. 1, 2012.

Izvorni znanstveni članak
https://doi.org/10.5562/cca2060

Binding Modes of Quinuclidinium Esters to Butyrylcholinesterase

Ines Primožič ; 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

Puni tekst: engleski, pdf (6 MB) str. 77-83 preuzimanja: 711* citiraj
APA 6th Edition
Primožič, I., Hrenar, T. i Tomić, S. (2012). Binding Modes of Quinuclidinium Esters to Butyrylcholinesterase. Croatica Chemica Acta, 85 (1), 77-83. https://doi.org/10.5562/cca2060
MLA 8th Edition
Primožič, Ines, et al. "Binding Modes of Quinuclidinium Esters to Butyrylcholinesterase." Croatica Chemica Acta, vol. 85, br. 1, 2012, str. 77-83. https://doi.org/10.5562/cca2060. Citirano 26.02.2021.
Chicago 17th Edition
Primožič, Ines, Tomica Hrenar i Srđanka Tomić. "Binding Modes of Quinuclidinium Esters to Butyrylcholinesterase." Croatica Chemica Acta 85, br. 1 (2012): 77-83. https://doi.org/10.5562/cca2060
Harvard
Primožič, I., Hrenar, T., i Tomić, S. (2012). 'Binding Modes of Quinuclidinium Esters to Butyrylcholinesterase', Croatica Chemica Acta, 85(1), str. 77-83. https://doi.org/10.5562/cca2060
Vancouver
Primožič I, Hrenar T, Tomić S. Binding Modes of Quinuclidinium Esters to Butyrylcholinesterase. Croatica Chemica Acta [Internet]. 2012 [pristupljeno 26.02.2021.];85(1):77-83. https://doi.org/10.5562/cca2060
IEEE
I. Primožič, T. Hrenar i S. Tomić, "Binding Modes of Quinuclidinium Esters to Butyrylcholinesterase", Croatica Chemica Acta, vol.85, br. 1, str. 77-83, 2012. [Online]. https://doi.org/10.5562/cca2060

Sažetak
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)

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

Hrčak ID: 80416

URI
https://hrcak.srce.hr/80416

Posjeta: 1.020 *