Discovery of novel α-glucosidase inhibitors based on the virtual screening with the homology-modeled protein structure

Bioorganic and Medicinal Chemistry

Volumn 16, Issue 1, 2008, Pages 284-292

  Park, Hwangseo ^a   Hwang, Kyo Yeol ^b   Oh, Kyung Hwan ^b   Kim, Young Hoon ^b   Lee, Jae Yeon ^b   Kim, Keun ^b  

^a Sejong University   (South Korea)

^b Suwon University   (South Korea)

Author keywords

glucosidase; Diabets; Docking; Enzyme assay; Homology modeling; Inhibitor; Virtual screening

Indexed keywords

4 NITROPHENYL ALPHA DEXTRO GLUCOPYRANOSIDE; ALPHA GLUCOSIDASE; ALPHA GLUCOSIDASE INHIBITOR; UNCLASSIFIED DRUG;

ARTICLE; COMPUTER AIDED DESIGN; COMPUTER ANALYSIS; DRUG SCREENING; ENZYME ACTIVE SITE; ENZYME INHIBITION; ENZYME INHIBITOR COMPLEX; IC 50; MOLECULAR MODEL; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY; STRUCTURE ACTIVITY RELATION;

ALPHA-GLUCOSIDASES; COMPUTER-AIDED DESIGN; DIABETES MELLITUS; DRUG DESIGN; ENZYME INHIBITORS; GLUCOSE METABOLISM DISORDERS; HUMANS; INHIBITORY CONCENTRATION 50; LIGANDS; PROTEIN BINDING; SOLVENTS; STRUCTURAL HOMOLOGY, PROTEIN; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 38049008981     PISSN: 09680896     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmc.2007.09.036     Document Type: Article

References (46)

1. Kimura A., Lee J.-H., Lee I.-S., Lee H.-S., Park K.-H., Chiba S., and Kim D. Carbohydr. Res. 339 (2004) 1035-1040
2. Heightman T.D., Andrea T., and Vasella A.T. Angew. Chem., Int. Ed. 38 (1999) 750-770
3. Robinson K.M., Begovic M.E., Rhinehart B.L., Heineke E.W., Ducep J.B., Kastner P.R., Marshall F.N., and Danzin C. Diabetes 40 (1991) 825-830
4. Braun C., Brayer G.D., and Withers S.G. J. Biol. Chem. 270 (1995) 26778-26781
5. Dwek R.A., Butters T.D., Platt F.M., and Nicole Zitzmann N. Nat. Rev. Drug Disc. 1 (2002) 65-75
6. Humphries M.J., Matsumoto K., White S.L., and Olden K. Cancer Res. 46 (1986) 5215-5222
7. Mehta A., Zitzmann N., Rudd P.M., Block T.M., and Dwek R.A. FEBS Lett. 430 (1998) 17-22
8. Karpas A., Fleet G.W.J., Dwek R.A., Petursson S., Namgoong S.K., Ramsden N.G., Jacob G.S., and Rademacher T.W. Proc. Natl. Acad. Sci. U.S.A. 85 (1988) 9229-9233
9. Zitzmann N., Mehta A.S., Carrouée S., Butters T.D., Platt F.M., McCauley J., Blumberg B.S., Dwek R.A., and Block T.M. Proc. Natl. Acad. Sci. U.S.A. 96 (1999) 11878-11882
10. Yee H.S., and Fong N.T. Pharmacotherapy 16 (1996) 792-805
11. de Melo E.B., Gomes A.S., and Carvalho I. Tetrahedron 62 (2006) 10277-10302
12. Lillelund V.H., Jensen H.H., Liang X., and Bols M. Chem. Rev. 102 (2002) 515-553
13. Xu H.-W., Dai G.-F., Liu G.-Z., Wang J.-F., and Liu H.-M. Bioorg. Med. Chem. 15 (2007) 4247-4255
14. Tanabe G., Yoshikai K., Hatanaka T., Yamamoto M., Shao Y., Minematsu T., Muraoka O., Wang T., Matsuda H., and Yoshikawa M. Bioorg. Med. Chem. 15 (2007) 3926-3937
15. Liu Y., Ma L., Chen W.-H., Wang B., and Xu Z.-L. Bioorg. Med. Chem. 15 (2007) 2810-2814
16. Pandey J., Dwivedi N., Singh N., Srivastava A.K., Tamarkar A., and Tripathi R.P. Bioorg. Med. Chem. Lett. 17 (2007) 1321-1325
17. Hakamata W., Nakanishi I., Masuda Y., Shimizu T., Higuchi H., Nakamura Y., Saito S., Urano S., Oku T., Ozawa T., Ikota N., Miyata N., Okuda H., and Fukuhara K. J. Am. Chem. Soc. 128 (2006) 6524-6525
18. Dai G.-F., Xu H.-W., Wang J.-F., Liu F.-W., and Liu H.-M. Bioorg. Med. Chem. Lett. 16 (2006) 2710-2713
19. Liu H., Sim L., Rose D.R., and Pinto B.M. J. Org. Chem. 71 (2006) 3007-3013
20. Seo W.D., Kim J.H., Kang J.E., Ryu H.W., Curtis-Long M.J., Lee H.S., Yang M.S., and Park K.H. Bioorg. Med. Chem. Lett. 15 (2005) 5514-5516
21. Luo J.-G., Wang X.-B., Ma L., and Kong L.-Y. Bioorg. Med. Chem. Lett. 17 (2007) 4460-4463
22. Saludes J.P., Lievens S.C., and Molinski T.F. J. Nat. Prod. 70 (2007) 436-438
23. Du Z.-Y., Liu R.-R., Shao W.-Y., Mao X.P., Ma L., Gu L.-Q., Huang Z.-S., and Chan A.S.C. Eur. J. Med. Chem. 41 (2006) 213-218
24. Lodge J.A., Maier T., Liebl W., Hoffmann V., and Sträter N. J. Biol. Chem. 278 (2003) 19151-19158
25. Rajan S.S., Yang X., Collart F., Yip V.L.Y., Withers S.G., Varrot A., Thompson J., Davies G.J., and Anderson W.F. Structure 12 (2004) 1619-1629
26. Zou X., Sun Y., and Kuntz I.D. J. Am. Chem. Soc. 121 (1999) 8033-8043
27. Shoichet B.K., Leach A.R., and Kuntz I.D. Proteins 34 (1999) 4-16
28. Baker D., and Sali A. Science 294 (2001) 93-96
29. Watanabe K., Hata Y., Kizaki H., Katsube Y., and Suzuki S. J. Mol. Biol. 269 (1997) 142-153
30. Nishio T., Hakamata W., Kimura A., Chiba S., Takatsuki A., Kawachi R., and Oku T. Carbohydr. Res. 337 (2002) 629-634
31. Tomich C.H., da Silva P., Carvalho I., and Taft C.A. J. Comput. Aided Mol. Des. 19 (2005) 83-92
32. Zhou J.-M., Zhou J.-H., Meng Y., and Chen M.-B. J. Chem. Theory Comput. 2 (2006) 157-165
33. Bairoch A., and Apweiler R. Nucleic Acids Res. 27 (1999) 49-54
34. Thompson J.D., Higgins D.G., and Gibson T.J. Nucleic Acids Res. 22 (1994) 4673-4680
35. Sali A., and Blundell T.L. J. Mol. Biol. 234 (1993) 779-815
36. Fiser A., Do R.K.G., and Sali A. Protein Sci. 9 (2000) 1753-1773
37. Sippl M.J. Proteins 17 (1993) 355-362
38. Morris G.M., Goodsell D.S., Halliday R.S., Huey R., Hart W.E., Belew R.K., and Olson A.J. J. Comput. Chem. 19 (1998) 1639-1662
39. Park H., Lee J., and Lee S. Proteins 65 (2006) 549-554
40. Jeffrey G.A. An Introduction to Hydrogen Bonding (1997), Oxford University Press, Oxford
41. Lipinski C.A., Lombardo F., Dominy B.W., and Feeney P.J. Adv. Drug Delivery Rev. 23 (1997) 3-25
42. Gasteiger J., and Marsili M. Tetrahedron 36 (1980) 3219-3228
43. Mehler E.L., and Solmajer T. Protein Eng. 4 (1991) 903-910
44. Stouten P.F.W., Frömmel C., Nakamura H., and Sander C. Mol. Simul. 10 (1993) 97-120
45. Kang H., Choi H., and Park H. J. Chem. Inf. Model. 47 (2007) 509-514
46. Roujeinikova A., Raasch C., Sedelnikova S., Liebl W., and Rice D.W. J. Mol. Biol. 321 (2002) 149-162