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Interaction of noncompetitive inhibitors with the alpha3beta2 nicotinic acetylcholine receptor investigated by affinity chromatography and molecular docking.

Abstract：

:A molecular model of the alpha3beta2 nAChR lumen channel was constructed and hydrophobic clefts were observed near the receptor gate. Docking simulations indicated that ligand-nAChR complexes were formed by hydrophobic interactions with the cleft and hydrogen bond interactions. The equilibrium constants and association and dissociation constant rates associated with the binding interactions were determined using nonlinear chromatography on an immobilized alpha3beta2 nAChR column. The computational-chromatography approach can be used to predict and describe ligand-nAChR interactions.

journal_name

J Med Chem

journal_title

Journal of medicinal chemistry

authors

Jozwiak K,Ravichandran S,Collins JR,Moaddel R,Wainer IW

doi

10.1021/jm070784s

subject

Has Abstract

pub_date

2007-11-29 00:00:00

pages

6279-83

issue

24

eissn

0022-2623

issn

1520-4804

journal_volume

50

pub_type

杂志文章

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