Interaction of Noncompetitive Inhibitors with the 32 Nicotinic Acetylcholine Receptor Investigated by Affinity Chromatography and Molecular Docking
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- 作者：Krzysztof Jozwiak ; Sarangan Ravichandran ; Jack R. Collins ; Ruin Moaddel ; Irving W. Wainer
- 刊名：Journal of Medicinal Chemistry
- 出版年：2007
- 出版时间：November 29, 2007
- 年：2007
- 卷：50
- 期：24
- 页码：6279 - 6283
- 全文大小：248K
- 年卷期：v.50,no.24(November 29, 2007)
- ISSN：1520-4804
文摘
A molecular model of the 32 nAChR lumen channel was constructed and hydrophobic clefts were observednear the receptor gate. Docking simulations indicated that ligand-nAChR complexes were formed byhydrophobic interactions with the cleft and hydrogen bond interactions. The equilibrium constants andassociation and dissociation constant rates associated with the binding interactions were determined usingnonlinear chromatography on an immobilized 32 nAChR column. The computational-chromatographyapproach can be used to predict and describe ligand-nAChR interactions.