Synthesis and the Intestinal Glucosidase Inhibitory Activity of 2-Aminoresorcinol Derivatives toward an Investigation of Its Binding Site | Zendy

Eisuke Kato | Zendy; Kenichi Oikawa | Zendy; Keisuke Takahashi | Zendy; Jun Kawabata | Zendy

Open Access

Synthesis and the Intestinal Glucosidase Inhibitory Activity of 2-Aminoresorcinol Derivatives toward an Investigation of Its Binding Site

Author(s) -

Eisuke Kato,

Kenichi Oikawa,

Keisuke Takahashi,

Jun Kawabata

Publication year - 2012

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.120009

Subject(s) - uncompetitive inhibitor , chemistry , inhibitory postsynaptic potential , stereochemistry , alkoxy group , methylation , structure–activity relationship , biochemistry , non competitive inhibition , enzyme , in vitro , organic chemistry , biology , alkyl , gene , neuroscience

2-Aminoresorcinol is a potent and selective intestinal glucosidase inhibitor. Unlike the majority of glucosidase inhibitors, it shows an uncompetitive mode of inhibition. In this study, we tested the intestinal glucosidase inhibitory activity of various 2-aminoresorcinol derivatives. We found that structural changes, in amino and two phenolic hydroxyl groups had a negative impact on inhibitory activity, but methylation of the phenolic hydroxyl group was found to maintain its activity and replacement of the aromatic ring with an acyl or alkoxy carbonyl group at the 4th position also retained its activity. This enable us to design a molecular probe for further study of the inhibition mechanism of 2-aminoresorcinol.

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