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K. Jones, L. Sim, S. Mohan, J. Kumarasamy, H. Liu, S. Avery, H. Y. Naim, R. Quezada-Calvillo, B. L. Nichols, B. M. Pinto and D. R. Rose, “Mapping the Intestinal Alpha-Glucogenic Enzyme Specificities of Starch Digesting Maltase-Glucoamylase and Sucrase-Isomaltase,” Bioorganic & Medicinal Chemistry, Vol. 19, No. 13, 2011, pp. 3929-3934. doi:10.1016/j.bmc.2011.05.033

has been cited by the following article:

• TITLE: Homology Modeling of Human Alpha-Glucosidase Catalytic Domains and SAR Study of Salacinol Derivatives

  AUTHORS: Shinya Nakamura, Kazunori Takahira, Genzoh Tanabe, Osamu Muraoka, Isao Nakanishi

  KEYWORDS: Homology Modeling; Docking Study; MM/PBSA; Alpha-Glucosidase; Salacinol; Kotalanol

  JOURNAL NAME: Open Journal of Medicinal Chemistry, Vol.2 No.3, September 27, 2012

  ABSTRACT: Maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) belong to human intestinal alpha-glucosidase and their N-terminal side catalytic domains are called NtMGAM and NtSI, and their C-terminal side catalytic domains are called CtMGAM and CtSI. As an antidiabetic, alpha-glucosidase inhibitor is required to bind to all of these domains to inhibit disaccharides hydrolysis. Salacinol and kotalanol isolated from Salacia reticulata are novel seed compounds for al-pha-glucosidase inhibitor. Even though the complex structures of NtMGAM or NtSI have been determined experimen-tally, those of CtMGAM and CtSI have not been revealed. Thus, homology modeling for CtMGAM and CtSI has been performed to predict the binding mode of salacinol and its derivatives for each domain. The binding affinities for these compounds were also calculated to explain the experimental structure-activity relationships (SARs). After a docking study of the derivatives to each catalytic domain, the MM/PBSA method has been applied to predict the binding affinities. The predicted binding affinities were almost consistent with the experimental SARs. The comparison of the complex structures and binding affinities provided insights for designing novel compounds, which inhibit all catalytic domains.