In silico analyses of essential interactions of iminosugars with the Hex A active site and evaluation of their pharmacological chaperone effects for Tay-Sachs disease

The affinity of a series of iminosugar-based inhibitors exhibiting various ring sizes toward Hex A and their essential interactions with the enzyme active site were investigated. All the Hex A-inhibiting iminosugars tested formed hydrogen bonds with Arg178, Asp322, Tyr421 and Glu462 and had the favo...

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Veröffentlicht in:	Organic & biomolecular chemistry 2017, Vol.15 (44), p.9297-9304
Hauptverfasser:	Kato, Atsushi, Nakagome, Izumi, Nakagawa, Shinpei, Kinami, Kyoko, Adachi, Isao, Jenkinson, Sarah F, Désiré, Jérôme, Blériot, Yves, Nash, Robert J, Fleet, George W J, Hirono, Shuichi
Format:	Artikel
Sprache:	eng
Schlagworte:	Catalysis Catalytic Domain Chemical bonds Chemical Sciences Clinical trials Computer Simulation Enzyme Inhibitors - chemistry Enzyme Inhibitors - metabolism Enzyme Inhibitors - pharmacology Enzyme Inhibitors - therapeutic use Hexosaminidase A - antagonists & inhibitors Hexosaminidase A - chemistry Hexosaminidase A - genetics Hexosaminidase A - metabolism Humans Hydrogen bonding Hydrogen bonds Medical research Medical treatment Molecular dynamics Molecular Dynamics Simulation Mutation Pharmacology Pyrimethamine Sugars - chemistry Sugars - metabolism Sugars - pharmacology Sugars - therapeutic use Tay-Sachs disease Tay-Sachs Disease - drug therapy Variation
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