BioFactors

Volume 41, Issue 4 p. 242-251

Research Communication

Screening alpha-glucosidase and alpha-amylase inhibitors from natural compounds by molecular docking in silico

Chien-Hung Jhong,

Chien-Hung Jhong

Institute of Biotechnology, National Dong-Hwa University, Hualien, 974 Taiwan

Search for more papers by this author

Jirawat Riyaphan,

Jirawat Riyaphan

Institute of Biotechnology, National Dong-Hwa University, Hualien, 974 Taiwan

Search for more papers by this author

Shih-Hung Lin,

Shih-Hung Lin

Institute of Biotechnology, National Dong-Hwa University, Hualien, 974 Taiwan

Search for more papers by this author

Yi-Chen Chia,

Yi-Chen Chia

Department of Food Science and Technology, Tajen University, Ping Tung Hsien, Taiwan

Search for more papers by this author

Ching-Feng Weng,

Corresponding Author

Ching-Feng Weng

Institute of Biotechnology, National Dong-Hwa University, Hualien, 974 Taiwan

Correspondence to: Ching-Feng Weng, Ph.D., Institute of Biotechnology, National Dong-Hwa University, Hualien 974, Taiwan. Tel.: +886-3-863-3637; Fax: +886-3-863-0255; E-mail: [email protected]Search for more papers by this author

Chien-Hung Jhong,

Chien-Hung Jhong

Institute of Biotechnology, National Dong-Hwa University, Hualien, 974 Taiwan

Search for more papers by this author

Jirawat Riyaphan,

Jirawat Riyaphan

Institute of Biotechnology, National Dong-Hwa University, Hualien, 974 Taiwan

Search for more papers by this author

Shih-Hung Lin,

Shih-Hung Lin

Institute of Biotechnology, National Dong-Hwa University, Hualien, 974 Taiwan

Search for more papers by this author

Yi-Chen Chia,

Yi-Chen Chia

Department of Food Science and Technology, Tajen University, Ping Tung Hsien, Taiwan

Search for more papers by this author

Ching-Feng Weng,

Corresponding Author

Ching-Feng Weng

Institute of Biotechnology, National Dong-Hwa University, Hualien, 974 Taiwan

First published: 07 July 2015

https://doi.org/10.1002/biof.1219

Citations: 100

Read the full text

About

PDF

Tools

Share a link

Email
Facebook
Twitter
LinkedIn
Reddit
Wechat

Abstract

The alpha-glucosidase inhibitor is a common oral anti-diabetic drug used for controlling carbohydrates normally converted into simple sugars and absorbed by the intestines. However, some adverse clinical effects have been observed. The present study seeks an alternative drug that can regulate the hyperglycemia by down-regulating alpha-glucosidase and alpha-amylase activity by molecular docking approach to screen the hyperglycemia antagonist against alpha-glucosidase and alpha-amylase activities from the 47 natural compounds. The docking data showed that Curcumin, 16-hydroxy-cleroda-3,13-dine-16,15-olide (16-H), Docosanol, Tetracosanol, Antroquinonol, Berberine, Catechin, Quercetin, Actinodaphnine, and Rutin from 47 natural compounds had binding ability towards alpha-amylase and alpha-glucosidase as well. Curcumin had a better biding ability of alpha-amylase than the other natural compounds. Analyzed alpha-glucosidase activity reveals natural compound inhibitors (below 0.5 mM) are Curcumin, Actinodaphnine, 16-H, Quercetin, Berberine, and Catechin when compared to the commercial drug Acarbose (3 mM). A natural compound with alpha-amylase inhibitors (below 0.5 mM) includes Curcumin, Berberine, Docosanol, 16-H, Actinodaphnine/Tetracosanol, Catechin, and Quercetin when compared to Acarbose (1 mM). When taken together, the implication is that molecular docking is a fast and effective way to screen alpha-glucosidase and alpha-amylase inhibitors as lead compounds of natural sources isolated from medicinal plants. © 2015 BioFactors, 41(4):242–251, 2015

References

1 WHO. (2013) Screening for Type 2 Diabetes, Report of a World Health Organization and International Diabetes Federation Meeting. Department of Noncommunicable Disease Manangement, Geneva, Switzerland, pp. 1–41.

Google Scholar
2Lin, C. C., Li, C. I., Hsiao, C. Y., Liu, C. S., Yang, S. Y., et al. (2013) Time trend analysis of the prevalence and incidence of diagnosed type 2 diabetes among adults in Taiwan from 2000 to 2007: a population-based study. BMC Public Health 13, 1–10.
10.1186/1471-2458-13-318
PubMedWeb of Science®Google Scholar
3Adi, S. and Andrea, G. G. (2012) Type 1 diabetes mellitus: an overview. Nutritional and Therapeutic Interventions for Diabetes and Metabolic Syndrome. Department of Pediatrics, Division of Pediatric Endocrinology, University of California, San Francisco CA. DOI: 10.1016/B978-0-12-385083-6.15001-6.
10.1016/B978‐0‐12‐385083‐6.15001‐6
Google Scholar
4Nair, S. S., Kavrekar, V., and Mishra, A. (2013) In vitro studies on alpha amylase and alpha glucosidase inhibitory activities of selected plant extracts. Eur. J. Exp. Biol. 3, 128–132.

Google Scholar
5Yee, H. S. and Fong, N. T. (1996) A review of the safety and efficacy of acarbose in diabetes mellitus. Pharmacotherapy 16, 792–805.
10.1002/j.1875-9114.1996.tb02997.x
CASPubMedWeb of Science®Google Scholar
6van de Laar, F. A. (2008) Alpha-glucosidase inhibitors in the early treatment of type 2 diabetes. Vasc. Health Risk Manage. 4, 1189–1195.
10.2147/VHRM.S3119
CASPubMedGoogle Scholar
7Kitchen, D. H., Furr, D. B., and Bajorath, J. R. J. (2004) Docking and scoring in virtual screening for drug discovery: methods and applications. Nat. Rev. Drug Discov. 3, 935–949.
10.1038/nrd1549
CASPubMedWeb of Science®Google Scholar
8Gilson, M. K. and Zhou, H. X. (2007) Calculation of protein-ligand binding affinities. Annu. Rev. Biophys. Biomol. Struct. 36, 21–42.
10.1146/annurev.biophys.36.040306.132550
CASPubMedWeb of Science®Google Scholar
9Xiaoyu Qing, X. Y. L., Raeymaeker J. D., Jeremy, R. H., T., Kam, Y. J. Z., Marc, D. M., et al., (2014) Pharmacophore modeling: advances, limitations, and current utility in drug discovery. J. Receptor Ligand Channel Res. 7, 81–92.

Google Scholar
10Yang, S. Y. (2010) Pharmacophore modeling and applications in drug discovery: challenges and recent advances. Drug Discov. Today 15, 444–450.
10.1016/j.drudis.2010.03.013
CASPubMedWeb of Science®Google Scholar
11Mukesh, K. R. B. (2011) Molecular docking: a review. IJRAP 2, 1746–1751.

Google Scholar
12Huang, Y. R. W. K. -F., Chang, E.-C., Chou, T.-L., and Wang, A. H. J. (2008) A conserved hydrogen-bond network in the catalytic centre of animal glutaminyl cyclases is critical for catalysis. Biochem. J., 411, 181–190.
10.1042/BJ20071073
CASPubMedWeb of Science®Google Scholar
13Brayer, Y. L. G. and Withers S. G. (1995) The structure of human pancreatic a-amylase at 1.8 A° resolution and comparisons with related enzymes. Protein Sci., 4, 1730–1742.
10.1002/pro.5560040908
CASPubMedWeb of Science®Google Scholar
14Tadera, K., Yuji, M., Kouta, T., and Tomoko, M., (2006) Inhibition of α-glucosidase and α-amylase by flavonoids. J. Nutr. Sci. Vitaminol., 52, 149–153.
10.3177/jnsv.52.149
CASPubMedWeb of Science®Google Scholar
15Mogale, M. A., Lebelo, S. L., Thovhogi, N., de Freitas, A. N., and Shai, L. J. (2011) α-amylase and α-glucosidase inhibitory effects of Sclerocarya birrea [(A. Rich.) Hochst.] subspecies caffra (Sond) Kokwaro (Anacardiaceae) stem-bark extracts. Afr. J. Biotechnol., 10, 15033–15039.
10.5897/AJB11.1408
CASWeb of Science®Google Scholar
16Venkatachalam, C. M., Jiang, X., Oldfield, T., and Waldman, M. (2003) LigandFit: a novel method for the shape-directed rapid docking of ligands to protein active sites. J. Mol. Graph. Model. 21, 289–307.
10.1016/S1093-3263(02)00164-X
CASPubMedWeb of Science®Google Scholar
17Wu, F., Xu, T., He, G., Ouyang, L., Han, B., et al. (2012) Discovery of novel focal adhesion kinase inhibitors using a hybrid protocol of virtual screening approach based on multicomplex-based pharmacophore and molecular docking. Int. J. Mol. Sci., 13, 15668–15678.
10.3390/ijms131215668
CASPubMedWeb of Science®Google Scholar
18 World Health Organization. (2012) Top 10 leading causes of death in the world 2000 and 2012. Available at: http://www.who.int/mediacentre/factsheets/fs310/en/. Accessed on May, 2014.

Google Scholar
19Wang, Z. D. H., Zhang, C., Tang, Z., He, Y., Zhang, Q., et al. (2014) Biological evaluation and 3D-QSAR studies of curcumin analogues as aldehyde dehydrogenase 1 inhibitors. J. Mol. Sci., 15, 8795–8807.
10.3390/ijms15058795
Web of Science®Google Scholar
20De Luca, J. M. O. C. (2008) Inflammation and insulin resistance. FEBS Lett. 582, 97–105.
10.1016/j.febslet.2007.11.057
CASPubMedWeb of Science®Google Scholar
21Hanefeld, F. S. M. (2008) Acarbose: oral antidiabetes drug with additional cardiovascular benefits. Expert Rev. Cardiovasc. Ther. 6, 153–163.
10.1586/14779072.6.2.153
PubMedGoogle Scholar
22Nakano, I. I. T., Seo, M., Takahashi, S., Komoda, T., and Katayama, S. (2009) Acarbose attenuates postprandial hyperlipidemia: investigation in an intestinal absortive cell model. Metabolism 58, 583–585.
10.1016/j.metabol.2009.02.003
CASPubMedWeb of Science®Google Scholar
23Yan, G. Z. J., Pan, J., and Wang, Y. (2014) α-glucosidase inhibition by luteolin: kinetics, interaction and molecular docking. Int. J. Biol. Macromol. 64, 213–223.
10.1016/j.ijbiomac.2013.12.007
CASPubMedWeb of Science®Google Scholar
24Curic, Y. W. S., Shan, B., Schaaf, C., Utpadel, D., Lange, M., et al. (2013) Curcumin acts anti-proliferative and pro-apoptotic in human meningiomas. J. Neurooncol. 113, 385–396.
10.1007/s11060-013-1148-9
CASPubMedWeb of Science®Google Scholar
25Wang, Z. D. H., Zhang, C., Tang, Z., He, Y., Zhang, Q., et al. (2014) Biological evaluation and 3D-QSAR studies of curcumin analogues as aldehyde dehydrogenase 1 inhibitors. J. Mol. Sci. 15, 8795–8807.
10.3390/ijms15058795
Web of Science®Google Scholar
26Jong-Sang, K., Chong-Suk, K., and Kun Ho, S. (2000) Inhibition of alpha-glucosidase and amylase by luteotin, a flavonoid. Biosci. Biotechnol. Biochem. 64, 2458–2461.
10.1271/bbb.64.2458
PubMedWeb of Science®Google Scholar
27Zhang, M. .F D.-W., Gao, S.-H. Liu, and, J.-L. (2013) Curcumin and diabetes: a systematic review. Evid. Based Complement. Alternat. Med. 2013, 1–16.

Google Scholar
28Stefanska, B. (2012) Curcumin ameliorates hepatic fibrosis in type 2 diabetes mellitus-insights into its mechanism of action. Br. J. Pharmacol. 166, 2209–2211.
10.1111/j.1476-5381.2012.01959.x
CASPubMedWeb of Science®Google Scholar
29Chiang, S. C. L. P. C., Pan, S. L., Kuo, C. H., Tsai, I.-L., Kuo, M. T., et al. (2010) Antroquinonol displays anticancer potential against human hepatocellular carcinoma cells: a crucial role of AMPK and mTOR pathways. Biochem. Pharmacol. 79, 167–171.
10.1016/j.bcp.2009.08.022
CASWeb of Science®Google Scholar
30Wang, Y. L. R. and Wang, S. (2003) Comparative evaluation of 11 scoring functions for molecular docking. J. Med. Chem. 46, 2287–2303.
10.1021/jm0203783
CASPubMedWeb of Science®Google Scholar
31Blundell, B. L. S. T. L., Montalvão, R. W., Brewerton, S., Chelliah, V., Worth, C. L., et al. (2006) Structural biology and bioinformatics in drug design: opportunities and challenges for target identification and lead discovery. Philos. Trans. R Soc. Lond. B Biol. Sci. 361, 413–423.
10.1098/rstb.2005.1800
CASPubMedWeb of Science®Google Scholar
32Sunand, D. O. S. H. (2010) Structure-based drug metabolism predictions for drug design. Chem. Biol. Drug Des. 75, 3–17.
10.1111/j.1747-0285.2009.00899.x
CASPubMedWeb of Science®Google Scholar
33Brindis, R. R. F., Bye, R., Gonzalez-Andrade, M., and Mata, R. (2011) (Z)−3-butylidenephthalide from Ligusticum porter, an α-glucosidase inhibitor. J. Nat. Prod. 74, 314–320.
10.1021/np100447a
CASPubMedWeb of Science®Google Scholar
34Yin, H. X. J. and Ye, J. (2008) Efficacy of berberine in patients with type 2 diabetes mellitus. Metabolism 57, 712–717.
10.1016/j.metabol.2008.01.013
CASPubMedWeb of Science®Google Scholar
35Daisy, K. B. P., Rajalakshmi, M., Eliza, J., and Selvaraj, J. (2010) Insulin mimetic impact of catechin isolated from Cassia fistula on the glucose oxidation and molecular mechanisms of glucose uptake on streptozotocin-induced diabetic Wistar rats. Phytomedicine 17, 28–36.
10.1016/j.phymed.2009.10.018
CASPubMedWeb of Science®Google Scholar
36Kumar, R. G. A. (2008) Quercetin protects against acute immobilization stress-induced behaviors and biochemical alterations in mice. J. Med. Food 11, 469–473.
10.1089/jmf.2006.0207
CASPubMedWeb of Science®Google Scholar
37Fernandes, E. L. B. N. A. A. H., Okoshi, K., Okoshi, M. P., Muzio, B. P. D., Guimarães, J. F. C., et al. (2010) Influence of rutin treatment on biochemical alterations in experimental diabetes. Biomed. Pharmacother. 64, 214–219.
10.1016/j.biopha.2009.08.007
CASPubMedWeb of Science®Google Scholar
38Yang, S. C. C. H. L., Lin, K. Y., Wang, M. T., Chen, Y. C., et al. (2011) Antioxidant activities of aqueous leaf extracts of Toona sinensis on free radical-induced endothelial cell damage. J. Ethnopharmacol. 137, 669–680.
10.1016/j.jep.2011.06.017
PubMedWeb of Science®Google Scholar
39Borges de Melo, A. D. S. G. E. and Carvalho, I. (2006) α- and β- glucosidase inhibitors: chemical structure and biological activity. Tetrahedron 62, 10277–10302.
10.1016/j.tet.2006.08.055
CASWeb of Science®Google Scholar
40Kim, C. S. K. J. S. and Son, K. H. (2000) Inhibition of alpha-glucosidase and amylase by luteolin, a flavonoid. Biosci. Biotechnol. Biochem. 64, 2458–2461.
10.1271/bbb.64.2458
CASPubMedWeb of Science®Google Scholar
41Kumar, S. N. S., Kumar, V., and Prakash, O. (2011) α-Glucosidase inhibitors from plants: a natural approach to treat diabetes. Pharmacogn. Rev. 5, 19–29.
10.4103/0973-7847.79096
CASPubMedGoogle Scholar

Citing Literature

Volume41, Issue4

July/August 2015

Pages 242-251

This article also appears in:

Screening alpha-glucosidase and alpha-amylase inhibitors from natural compounds by molecular docking in silico

Abstract

References

Citing Literature

References

Information

About Wiley Online Library

Help & Support

Opportunities

Connect with Wiley

Screening alpha-glucosidase and alpha-amylase inhibitors from natural compounds by molecular docking in silico

Abstract

References

Citing Literature

References

Related

Information