In silico characterization of cytisinoids docked into an acetylcholine binding protein

Cytisine and several derivatives docked into an acetylcholine binding protein of Lymnaea stagnalis (Ls-AChBP), taken as a model of the agonist binding site of neuronal nicotinic acetylcholine receptor (nAChR). A strong correlation was found between the docking energies and experimental pIC50 values....

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Veröffentlicht in:	Bioorganic & medicinal chemistry letters 2010-06, Vol.20 (12), p.3683-3687
Hauptverfasser:	Abin-Carriquiry, Juan Andrés, Zunini, Margot Paulino, Cassels, Bruce K., Wonnacott, Susan, Dajas, Federico
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetylcholine binding protein Alkaloids - chemistry Animals Azocines - chemistry Biological and medical sciences Carrier Proteins - chemistry Carrier Proteins - metabolism Cholinergic system Computer Simulation Crystallization Cytisinoids Docking Lymnaea Medical sciences Molecular Structure Neuropharmacology Neurotransmitters. Neurotransmission. Receptors Nicotine - chemistry Nicotinic acetylcholine receptors Pharmacology. Drug treatments Protein Binding Pyridones - chemistry Quinolizines - chemistry Receptors, Nicotinic - chemistry Receptors, Nicotinic - metabolism X-Ray Diffraction
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