Article citationsMore>>
Tanabe, G., Xie, W., Balakishan, G., Amer, M.F., Tsutsui, N., Takemura, H., Nakamura, S., Akaki, J., Ninomiya, K., Morikawa, T., Nakanishi, I. and Muraoka, O. (2016) Hydrophobic Substituents Increase the Potency of Salacinol, a Potent α-Glucosidase Inhibitor from Ayurvedic Traditional Medicine “Salacia”. Bioorganic & Medicinal Chemistry, 24, 3705-3715.
https://doi.org/10.1016/j.bmc.2016.06.013
has been cited by the following article:
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TITLE:
Computational Study on the Comparative Differences in the Activity of Inhibitors of Human versus Rat Alpha-Glucosidase
AUTHORS:
Shinya Nakamura, Kazuko Shimada, Genzoh Tanabe, Osamu Muraoka, Isao Nakanishi
KEYWORDS:
Homology Modeling, MM/PBSA, Alpha-Glucosidase, Salacinol, Acarbose, Species Difference
JOURNAL NAME:
Open Journal of Medicinal Chemistry,
Vol.7 No.2,
June
15,
2017
ABSTRACT: Differences between the inhibitory activities of specific compounds on analogous enzymes isolated from different animal species are one of the critical issues to evaluate when exploring structure-activity relationships. The activity of acarbose is about ten times stronger in rat than in human, and that of neosalacinol is similar in both species. Binding affinities of acarbose and neosalacinol to four catalytic domains of alpha-glucosidases in human and rat were compared to investigate the cause of activity differences among species. Species difference was brought about complicatedly by the balance of interaction with four domains, and the result was indicated that larger ligand would show larger species difference in activity.
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