942610-80-2Relevant articles and documents
Biological evaluation of de-O-sulfonated analogs of salacinol, the role of sulfate anion in the side chain on the α-glucosidase inhibitory activity
Tanabe, Genzoh,Yoshikai, Kazuya,Hatanaka, Takanori,Yamamoto, Mizuho,Shao, Ying,Minematsu, Toshie,Muraoka, Osamu,Wang, Tao,Matsuda, Hisashi,Yoshikawa, Masayuki
, p. 3926 - 3937 (2008/02/13)
De-O-sulfonated analogs (10a, Y- = CH3OSO3 and 10b, Y- = Cl) of salacinol, a naturally occurring glycosidase inhibitor, and its diastereomer (12a, Y- = CH3OSO3) with l-thiosugar moiety (1,4-dideoxy-1,4-epithio-l-arabinitol) were prepared. Their inhibitory activities against intestinal maltase and sucrase were examined and compared with those of the parent α-glycosidase inhibitor, salacinol (1a). Compounds 10a and 10b showed a potent inhibitory activity equal to that of 1a against both enzymes, although 12a was a weak inhibitor against sucrase and maltase. These results indicated that the O-sulfonate anion moiety of 1a is not essential for the inhibitory activity.