Article
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.
Organic & biomolecular chemistry - 15 Nov 2017
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
Abstract excerpt
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 favorable cation-π interaction with Trp460. Among them, DMDP amide (6) proved to be the most potent competitive...
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