Inhibition kinetics of flavonoids on yeast α-glucosidase merged with docking simulations

Protein and Peptide Letters

Volumn 17, Issue 10, 2010, Pages 1270-1279

  Xu, Heng ^a  

^a JIAYING UNIVERSITY   (China)

Author keywords

Autodock; Flavonoid; Fluorescence quenching; Inhibition kinetics

Indexed keywords

ALPHA GLUCOSIDASE; FLAVONOID; QUERCETIN;

AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; COMPUTER SIMULATION; DRUG ANTAGONISM; DRUG EFFECT; ENZYMOLOGY; KINETICS; METABOLISM; MOLECULAR GENETICS; PROTEIN BINDING; SACCHAROMYCES CEREVISIAE; SEQUENCE ALIGNMENT; SPECTROFLUOROMETRY;

ALPHA-GLUCOSIDASES; AMINO ACID SEQUENCE; COMPUTER SIMULATION; FLAVONOIDS; KINETICS; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; QUERCETIN; SACCHAROMYCES CEREVISIAE; SEQUENCE ALIGNMENT; SPECTROMETRY, FLUORESCENCE;

EID: 77958483943     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986610792231492     Document Type: Article

References (62)

1. Noguchi, A.; Yano, M.; Ohshima, Y.; Hemmi, H.; Inohara-Ochiai, M.; Okada, M.; Min, K. S.; Nakayama, T.; Nishino, T. Deciphering themolecular basis of the broad substrate specificity of alphaglucosidase from Bacillus sp SAM1606. J. Biochem., 2003, 134, 543-550.
2. Henrissat, B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J., 1991, 280, 309-316.
3. Jespersen, H. M.; MacGregor, E. A.; Sierks, M. R.; Svensson, B. Comparison of the domain-level organization of starch hydrolases and related enzymes. Biochem. J., 1991, 280, 51-55.
4. Jespersen, H. M.; MacGregor, E. A.; Henrissat, B.; Sierkes, M. R.; Svensson, B. Starch and glycogen-debranching and branching enzymes: Prediction of structural features of the catalytic (β/α)8-barrel domain and evolutionary relationship to other amylolytic enzymes. J. Protein Chem., 1993, 12, 791-805.
5. Svensson, B. Protein engineering in the α-amylase family: catalytic mechanism, substrate specificity, and stability. Plant Mol. Biol., 1994, 25, 141-157.
6. Watanabe, J.; Kawabata, J.; Kurihara, H.; Niki, R. Isolation and identification of alpha-glucosidase inhibitors from Tochu-cha (Eucommia ulmoides). Biosci., Biotechnol., Biochem., 1997, 61(1), 177-178.
7. Suresh Babu, K.; Tiwari, A. K.; Srinivas, P. V.; Ali, A. Z.; China Raju, B.; Rao, J. M. Yeast and mammalian α-glucosidase inhibitory constituents from Himalayan rhubarb Rheum emodi Wall. ex Meisson. Bioorg. Med. Chem. Lett., 2004, 14, 3841-3845.
8. Matsui, T.; Yoshimoto, C.; Osajima, K.; Oki, T.; Osajima, Y. In vitro survey of α-glucosidase inhibitory food components. Biosci., Biotechnol., Biochem., 1996, 60(12), 2019-2022.
9. Subramanian, R.; Asmawi, M. Z.; Sadikun, A. In vitro alpha glucosidase and alpha amylase enzyme inhibitory effects of Andrographis paniculata extract and andrographolide. Acta Biochim. Pol., 2008, 55, 391-398.
10. Chen, H. M.; Zheng, L.; Yan, X. J. The preparation and bioactivity research of agaro-oligosaccharides. Food Technol. Biotechnol., 2005, 43(1), 29-36.
11. Kim, J. S.; Kwon, C. S.; Son, K. H. Inhibition of Alpha-glucosidase and Amylase by Luteolin, a Flavonoid. Biosci., Biotechnol., Biochem., 2000, 64(11), 2458-2461.
12. Park, H.; Hwang, K. Y.; Oh, K. H.; Kim, Y. H.; Lee, J. Y.; Kim, K. Discovery of novel α-glucosidase inhibitors based on the virtual screening with the homology-modeled protein structure. Bioorg. Med. Chem., 2008, 16(1), 284-292.
13. Rusznyak, S.; Szent-Györgyi, A. Vitamin P: flavonols as vitamins. Nature, 1936, 138, 27-27.
14. Cheong, H.; Ryu, S. Y.; Oak, M. H.; Cheon, S. H.; Yoo, G. S.; Kim, K. M. Studies of structure activity relationship of flavonoids for the anti-allergic actions. Arch. Pharmacal Res., 1998, 21(4), 478-480.
15. Yamamoto, Y.; Gaynor, R. B. Therapeutic potential of inhibition of the NF-κB pathway in the treatment of inflammation and cancer. J. Clin. Invest., 2001, 107(2), 135-142.
16. Gábor, M. Anti-inflammatory and anti-allergic properties of flavonoids. Prog. Clin. Biol. Res., 1986, 213, 471-480.
17. Cushnie, T. P. T.; Lamb, A. J. Antimicrobial activity of flavonoids. Int. J. Antimicrob. Agents, 2005, 26(5), 343-356.
18. Birt, D. F.; Hendrich, S.; Wang, W. Dietary agents in cancer prevention: flavonoids and isoflavonoids. Pharmacol. Ther., 2001, 90(2-3), 157-177.
19. Yochum, L.; Kushi, L. H.; Meyer, K.; Folsom, A. R. Dietary flavonoid intake and risk of cardiovascular disease in postmenopausal women. Climacteric, 1999, 2(3), 237-238.
20. Yao, L. H.; Jiang, Y. M.; Shi, J.; TomÁS-BarberÁN, F. A.; Datta, N.; Singanusong, R.; Chen, S. S. Flavonoids in Food and Their Health Benefits. Qual. Plant. - Plant Foods Hum. Nutr, 2004, 59(3), 113-122.
21. Tadera, K.; Minami, Y.; Takamatsu, K.; Matsuoka, T. Inhibition of α-glucosidase and α-amylase by flavonoids. J. Nutr. Sci. Vitaminol., 2006, 52(2), 149-153.
22. Chapdelaine, P.; Tremblay, R. R.; Dube, J. Y. p-Nitrophenol-alpha-D-glucopyranoside as substrate for measurement of maltase activity in human semen. Clin. Chem. (Washington, DC, U. S.), 1978, 24(2), 208-211.
23. Wu, X. Q.; Wang, J.; Lü, Z. R.; Tang, H. M.; Park, D.; Oh, S. H.; Bhak, J.; Shi, L.; Park, Y. D.; Zou, F. Alpha-Glucosidase Folding During Urea Denaturation: Enzyme Kinetics and Computational Prediction. Appl. Biochem. Biotechnol., 2009, 160(5), 1341-1355.
24. Lakowicz, J. R. Principles of Fluorescence Spectroscopy. Plenum Press: New York, 1983.
25. Sharma, A.; Schulman, S. G. Introduction to Fluorescence Spectroscopy. Wiley-Interscience: New York, 1999.
26. Lehrer, S. S. Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry, 1971, 10(17), 3254-3263.
27. Bi, S.; Song, D.; Tian, Y.; Zhou, X.; Liu, Z.; Zhang, H. Molecular spectroscopic study on the interaction of tetracyclines with serum albumins. Spectrochim. Acta, Part A, 2005, 61(4), 629-636.
28. Guex, N.; Peitsch, M. C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis, 1997, 18(15), 2714-2723.
29. Bairoch, A.; Apweiler, R. The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1999. Nucleic Acids Res., 1999, 27(1), 49-54.
30. Ghaemmaghami, S.; Huh, W. K.; Bower, K.; Howson, R. W.; Belle, A.; Dephoure, N.; O'Shea, E. K.; Weissman, J. S. Global analysis of protein expression in yeast. Nature, 2003, 425(6959), 737-741.
31. Watanabe, K.; Hata, Y.; Kizaki, H.; Katsube, Y.; Suzuki, Y. The refined crystal structure of Bacillus cereus oligo-1, 6-glucosidase at 2.0 Å resolution: structural characterization of proline-substitution sites for protein thermostabilization. J. Mol. Biol., 1997, 269(1), 142-153.
32. Ware, W. R. Oxygen quenching of fluorescence in solution: an experimental study of the diffusion process. J. Phys. Chem., 1962, 66 (3), 455-458.
33. Tian, J.; Liu, J.; He, W.; Hu, Z.; Yao, X.; Chen, X. Probing the binding of scutellarin to human serum albumin by circular dichroism, fluorescence spectroscopy, FTIR, and molecular modeling method. Biomacromolecules, 2004, 5(5), 1956-1961.
34. Morris, G. M.; Goodsell, D. S.; Halliday, R. S.; Huey, R.; Hart, W. E.; Belew, R. K.; Olson, A. J. Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J. Comput. Chem., 1998, 19(14), 1639-1662.
35. Iio, M.; Yoshioka, A.; Imayoshi, Y.; Koriyama, C.; Moriyama, A. Effect of flavonoids on α-glucosidase and β-fructosidase from yeast. Agric. Biol. Chem., 1984, 48, 1559-1563.
36. Hu, Y.; Liu, Y.; Shen, X.; Fang, X.; Qu, S. Studies on the interaction between 1-hexylcarbamoyl-5-fluorouracil and bovine serum albumin. J. Mol. Struct., 2005, 738(1), 143-147.
37. Wu, X. Q.; Zhu, W. J.; Lü, Z. R.; Xia, Y.; Yang, J. M.; Zou, F.; Wang, X. Y. The effect of rutin on arginine kinase: Inhibition kinetics and thermodynamics merging with docking simulation. Int. J. Biol. Macromol., 2009, 44(2), 149-155.
38. Huang, R. B.; Du, Q. S.; Wang, C. H.; Chou, K. C. An in-depth analysis of the biological functional studies based on the NMR M2 channel structure of influenza A virus. Biochem. Biophys. Res. Commun., 2008, 377(4), 1243-1247.
39. Du, Q. S.; Huang, R. B.; Wang, C. H.; Li, X. M.; Chou, K. C. Energetic analysis of the two controversial drug binding sites of the M2 proton channel in influenza A virus. J. Theor. Biol., 2009, 259(1), 159-164.
40. Schnell, J. R.; Chou, J. J. Structure and mechanism of the M2 proton channel of influenza A virus. Nature, 2008, 451(7178), 591-595.
41. Pielak, R. M.; Schnell, J. R.; Chou, J. J. Mechanism of drug inhibition and drug resistance of influenza A M2 channel. Proc. Natl. Acad. Sci. U. S. A., 2009, 106(18), 7379.
42. Chou, K. C. Review: Structural bioinformatics and its impact to biomedical science. Curr. Med. Chem., 2004, 11(16), 2105-2134.
43. Chou, K. C. Molecular therapeutic target for type-2 diabetes. J. Proteome Res., 2004, 3(6), 1284-1288.
44. Wei, D. Q.; Wang, J. F.; Chen, C.; Li, Y.; Chou, K. C. Molecular modeling of two CYP2C19 SNPs and its implications for personalized drug design. Protein Pept. Lett., 2008, 15(1), 27-32.
45. Du, Q. S.; Huang, R. B.; Wang, S. Q.; Chou, K. C. Designing Inhibitors of M2 Proton Channel against H1N1 Swine Influenza Virus. PLoS One, 2010, 5(2), e9388.
46. Wang, J. F.; Yan, J. Y.; Wei, D. Q.; Chou, K. C. Binding of CYP2C9 with diverse drugs and its implications for metabolic mechanism. Med. Chem., 2009, 5(3), 263-270.
47. Chou, K. C.; Wei, D. Q.; Zhong, W. Z. Binding mechanism of coronavirus main proteinase with ligands and its implication to drug design against SARS. Biochem. Biophys. Res. Commun., 2003, 308(1), 148-151.
48. Chou, K. C.; Wei, D. Q.; Du, Q. S.; Sirois, S.; Zhong, W. Z. Review: Progress in computational approach to drug development against SARS. Curr. Med. Chem., 2006, 13(27), 3263-3270.
49. Wei, D. Q.; Sirois, S.; Du, Q. S.; Arias, H. R.; Chou, K. C. Theoretical studies of Alzheimer's disease drug candidate 3-[(2, 4-dimethoxy) benzylidene]-anabaseine (GTS-21) and its derivatives. Biochem. Biophys. Res. Commun., 2005, 338(2), 1059-1064.
50. Zhang, R.; Wei, D. Q.; Du, Q. S.; Chou, K. C. Molecular modeling studies of peptide drug candidates against SARS. Med. Chem., 2006, 2(3), 309-314.
51. Wang, J. F.; Chou, K. C. Insight into the molecular switch mechanism of human Rab5a from molecular dynamics simulations. Biochem. Biophys. Res. Commun., 2009, 390(3), 608-612.
52. Baker, D.; Sali, A. Protein structure prediction and structural genomics. Science, 2001, 294(5540), 93-96.
53. Kimura, A. Molecular Anatomy of α-Glucosidase. Trends Glycosci. Glycotechnol., 2000, 12, 373-380.
54. Thompson, J. D.; Gibson, T. J.; Plewniak, F.; Jeanmougin, F.; Higgins, D. G. The CLUSTAL_X windows interface: flexiblestrategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res., 1997, 25(24), 4876-4882.
55. Chou, K. C.; Watenpaugh, K. D.; Heinrikson, R. L. A model of the complex between cyclin-dependent kinase 5 and the activation domain of neuronal Cdk5 activator. Biochem. Biophys. Res. Commun., 1999, 259(2), 420-428.
56. Zhang, J.; Luan, C. H.; Chou, K. C.; Johnson, G. V. W. Identification of the N-terminal functional domains of Cdk5 by molecular truncation and computer modeling. Proteins: Struct. Funct. Bioinf., 2002, 48(3), 447-453.
57. Chou, K. C. Insights from modelling the 3D structure of the extracellular domain of alpha 7 nicotinic acetylcholine receptor. Biochem. Biophys. Res. Commun., 2004, 319(2), 433-438.
58. Wei, D. Q.; Du, Q. S.; Sun, H.; Chou, K. C. Insights from modeling the 3D structure of H5N1 influenza virus neuraminidase and its binding interactions with ligands. Biochem. Biophys. Res. Commun., 2006, 344(3), 1048-1055.
59. Wang, S. Q.; Du, Q. S.; Chou, K. C. Study of drug resistance of chicken influenza A virus (H5N1) from homology-modeled 3D structures of neuraminidases. Biochem. Biophys. Res. Commun., 2007, 354(3), 634-640.
60. Du, Q. S.; Sun, H.; Chou, K. C. Inhibitor Design for SARS Coronavirus Main Protease Based on Distorted Key Theory. Med. Chem., 2007, 3(1), 1-6.
61. Housaindokht, M. R.; Bozorgmehr, M. R.; Bahrololoom, M. Analysis of ligand binding to proteins using molecular dynamics simulations. J. Theor. Biol., 2008, 254(2), 294-300.
62. Chiba, S. Molecular mechanism in alpha-glucosidase and glucoamylase. Biosci., Biotechnol., Biochem., 1997, 61(8), 1233-1239.