Docking Sulochrin and Its Derivative as α-Glucosidase Inhibitors of Saccharomyces cerevisiae

Wening Lestari(1*), Rizna Triana Dewi(2), Leonardus Broto Sugeng Kardono(3), Arry Yanuar(4)

(1) Center for Radioisotopes and Radiopharmaceuticals Technology, National Nuclear Energy Agency, Puspiptek, Serpong 15314
(2) Research Center for Chemistry, Indonesian Institute of Sciences, Puspiptek, Serpong 15314
(3) Research Center for Chemistry, Indonesian Institute of Sciences, Puspiptek, Serpong 15314
(4) Faculty of Pharmacy, Universitas Indonesia, Depok 16424
(*) Corresponding Author


Sulochrin is known to have an activity as inhibitors of the α-glucosidase enzyme. In this report interaction of sulochrin to the active site of the α-glucosidase enzyme from Saccharomyces cerevisiae was studied by docking method. The crystal structure of α-glucosidase from S. cerevisiae obtained from the homology method using α-glucosidase from S. cerevisiae (Swiss-Prot code P53341) as a target and crystal structure of isomaltase from S. cerevisiae (PDB code 3A4A) as a template. These studies show that sulochrin and sulochrin-I could be bound in the active site of α-glucosidase from S. cerevisiae through the formation of hydrogen bonds with Arg213, Asp215, Glu277, Asp352. Sulochrin-I has stability and inhibition of the α-glucosidase enzyme better than sulochrin. The iodine atom in the structure of sulochrin can increase the activity as an inhibitor of the α-glucosidase enzyme.


sulochrin; sulochrin-I; α-glucosidase inhibitor; S. cerevisiae

Full Text:

Full Text Pdf


[1] Li, Y., Wen, S., Kota, B.P., Peng, G., Li, G.Q., Yamahara, J., and Roufogalis, B.D., 2005, Punica granatum flower extract, a potent alpha-glucosidase inhibitor, improves postprandial hyperglycemia in Zucker diabetic fatty rats, J. Ethnopharmacol., 99 (2), 239–244.

[2] Kim, Y.M., Jeong, Y.K., Wang, M.H., Lee, W.Y., and Rhee, H.I., 2005, Inhibitory effect of pine extract on α-glucosidase activity and postprandial hyperglycemia, Nutrition, 21 (6), 756–761.

[3] van de Laar, F.A., Lucassen, P.L., Akkermans, R.P., van de Lisdonk, E.H., Rutten, G.E., and van Weel, C., 2005, α-glucosidase inhibitors for patients with type 2 diabetes results from a Cochrane systematic review and meta-analysis, Diabetes Care, 28 (11), 154–163.

[4] Zeng, Y.F., Lu, Z.R., Yan, L., Oh, S., Yang, J.M., Lee, J., and Ye, Z.M., 2012, Towards alpha-glucosidase folding induced by trifluoroethanol: Kinetics and computational prediction, Process Biochem., 47 (12), 2284–2290.

[5] Gao, H., Huang, Y.N., Gao, B., Li, P., Inagaki, C., and Kawabata, J., 2008, Inhibitory effect on α-glucosidase by Adhatoda vasica Nees, Food Chem., 108 (3), 965–972.

[6] Bharatham, K., Bharatham, N., Park, K.H., and Lee, K.W., 2008, Binding mode analyses and pharmacophore model development for sulfonamide chalcone derivatives, a new class of α-glucosidase inhibitors, J. Mol. Graphics Modell., 26, 1202–1212.

[7] Saqib, U., and Siddiqi, M.I., 2008, Probing ligand binding interactions of human alpha glucosidase by homology modeling and molecular docking, Int. J. Integr. Biol., 2 (2), 116–121.

[8] Park, H., Hwang, K.Y., Kim, Y.H., Oh, K.H., Lee, J.Y., and Kim, K., 2008, Discovery of novel alpha-glucosidase inhibitors based on the virtual screening with the homology-modeled protein structure, Bioorg. Med. Chem., 16 (1), 284–292.

[9] Nakamura, S., Takahira, K., Tanabe, G., Morikawa, T., Sakano, M., Ninomiya, K., Yoshikawa, M., Muraoka, O., and Nakanishi, I., 2010, Docking and SAR studies of salacinol derivatives as α-glucosidase inhibitors, Bioorg. Med. Chem. Lett., 20 (15), 4420–4423.

[10] Dewi, R.T., Anita, Y., Istyastono, E.P., Darmawan, A., and Hanafi, M., 2009, The applicability of the crystal structure of Termotoga maritima 4-a-glucanotransferase as the template for sulochrin as a-glucosidase inhibitors, Indones. J. Chem., 9 (3), 487–490.

[11] Farkhani, A., 2012, Molecular Dynamic Analysis of Docking Product of Complex α-Glucosidase with Sulochrin, Undergraduate Thesis, Universitas Indonesia, 35-38.

[12] Lestari, W., Susilo, V.Y., Setiyowati, S., Triningsih, Ariyanto, A., Widayati, P., Kardono, L.B.S., and Yannuar, A., 2014, Synthesis of sulochrin-125I and its binding affinity as α-glucosidase inhibitor using Radioligand Binding Assay (RBA) method, Atom Indonesia, 40 (1), 22–26.

[13] Lestari, W., 2013, Synthesis and Binding Study Sulochrin-125I as α-glucosidase Inhibitor using Radioligand Binding Assay (RBA) and Molecular Docking Methods, Thesis, Universitas Indonesia, 42.

[14] Arnold, K., Bordoli, L., Kopp, J., and Schwede, T., 2006, The SWISS-MODEL workspace: A web-based environment for protein structure homology modeling, Bioinformatics, 22 (2), 195–201.

[15] Kiefer, F., Arnold, K., Künzli, M., Bordoli, L., and Schwede, T., 2009, The SWISS-MODEL Repository and associated resources, Nucleic Acids Res., 37, D387–D392.

[16] Yamamoto, K., Miyake, H., Kusunoki, M., and Osaki, S., 2010, Crystal structures of isomaltase from Saccharomyces cerevisiae and in complex with its competitive inhibitor maltose, FEBS J., 277 (20), 4205–4214.

[17] Benkert, P., Biasini, M., and Schwede, T., 2010, Toward the estimation of the absolute quality of individual protein structure models, Bioinformatics, 27 (3), 343–350.

[18] Rasouli, H. and Fazeli-Nasab, B., 2014, Structural validation and homology modeling of LEA 2 protein in bread wheat, American-Eurasian J. Agric. Environ. Sci., 14 (10), 1044–1048.

[19] Rahman, M.A., Chaturvedi, N., Sinha, S., Pandey, P.A., Gupta, D.K., Sundaram, S., and Tripathi, A., 2013, Computational protein structure modeling and analysis of UV-B stress protein in Synechocystis PCC 6803, Bioinformation, 9 (12), 639–644.


Article Metrics

Abstract views : 3797 | views : 4161

Copyright (c) 2017 Indonesian Journal of Chemistry

Creative Commons License
This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.


Indonesian Journal of Chemistry (ISSN 1411-9420 /e-ISSN 2460-1578) - Chemistry Department, Universitas Gadjah Mada, Indonesia.

Analytics View The Statistics of Indones. J. Chem.