Flavonoids for controlling starch digestion: Structural requirements for inhibiting human α-amylase

Journal of Medicinal Chemistry

Volumn 51, Issue 12, 2008, Pages 3555-3561

  Lo Piparo, Elena ^a   Scheib, Holger ^a   Frei, Nathalie ^a   Williamson, Gary ^a   Grigorov, Martin ^a   Chou, Chieh Jason ^a  

^a NESTLÉ RESEARCH CENTER   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

ACACETIN; AMYLASE; CATECHIN; DAIDZEIN; DIOSMETIN; EPICATECHIN; EUPAFOLIN; FISETIN; FLAVONE DERIVATIVE; FLAVONOID; FLAVONOL DERIVATIVE; GENISTEIN; GENKWANIN; HESPERETIN; HYDROXYL GROUP; ISORHAMNETIN; KAEMPFEROL; LUTEOLIN; MYRICETIN; NARINGENIN; POLYPHENOL; QUERCETAGETIN; QUERCETIN; RHAMNETIN; SCUTELLAREIN; STARCH;

ARTICLE; BINDING SITE; DIGESTION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME INHIBITOR INTERACTION; GLUCOSE BLOOD LEVEL; HUMAN; HYDROGEN BOND; IC 50; POSTPRANDIAL STATE; STRUCTURE ACTIVITY RELATION;

ALPHA-AMYLASE; CATALYTIC DOMAIN; DIGESTION; FLAVONES; FLAVONOLS; HUMANS; HYDROGEN BONDING; LIGANDS; MODELS, MOLECULAR; PROTEIN CONFORMATION; SALIVA; STARCH; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 45749116594     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm800115x     Document Type: Article

References (32)

1. Henrissat, B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 1991, 280 (Part 2), 309-316.
2. Brayer, G. D.; Sidhu, G.; Maurus, R.; Rydberg, E. H.; Braun, C.; Wang, Y.; Nguyen, N. T.; Overall, C. M.; Withers, S. G. Subsite mapping of the human pancreatic alpha-amylase active site through structural, kinetic, and mutagenesis techniques. Biochemistry 2000, 39, 4778-4791.
3. Groot, P. C.; Bleeker, M. J.; Pronk, J. C.; Arwert, F.; Mager, W. H.; Planta, R. J.; Eriksson, A. W.; Frants, R. R. Human pancreatic amylase is encoded by two different genes. Nucleic Acids Res. 1988, 16, 4724.
4. Gumucio, D. L.; Wiebauer, K.; Caldwell, R. M.; Samuelson, L. C.; Meisler, M. H. Concerted evolution of human amylase genes. Mol. Cell. Biol. 1988, 8, 1197-1205.
5. Brayer, G. D.; Luo, Y.; Withers, S. G. The structure of human pancreatic alpha-amylase at 1.8 Å resolution and comparisons with related enzymes. Protein Sci. 1995, 4, 1730-1742.
6. Ramasubbu, N.; Paloth, V.; Luo, Y.; Brayer, G. D.; Levine, M. J. Structure of human salivary alpha-amylase at 1.6 A resolution: implications for its role in the oral cavity. Acta Crystallogr., Sect. D.: Biol. Crystallogr. 1996, 52, 435-446.
7. Al Kazaz, M.; Desseaux, V.; Marchis-Mouren, G.; Prodanov, E.; Santimone, M. The mechanism of porcine pancreatic alpha-amylase. Inhibition of maltopentaose hydrolysis by acarbose, maltose and maltotriose. Eur. J. Biochem. 1998, 252, 100-107.
8. Kim, M. J.; Lee, S. B.; Lee, H. S.; Lee, S. Y.; Baek, J. S.; Kim, D.; Moon, T. W.; Robyt, J. F.; Park, K. H. Comparative study of the inhibition of alpha-glucosidase, alpha-amylase, and cyclomaltodextrin glucanosyltransferase by acarbose, isoacarbose, and acarviosine-glucose. Arch. Biochem. Biophys. 1999, 371, 277-283.
9. Lankisch, M.; Layer, P.; Rizza, R. A.; DiMagno, E. P. Acute postprandial gastrointestinal and metabolic effects of wheat amylase inhibitor (WAI) in normal, obese, and diabetic humans. Pancreas 1998, 17, 176-181.
10. Boivin, M.; Flourie, B.; Rizza, R. A.; Go, V. L.; DiMagno, E. P. Gastrointestinal and metabolic effects of amylase inhibition in diabetics. Gastroenterology 1988, 94, 387-394.
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, 2458-2461.
12. McDougall, G. J.; Shpiro, F.; Dobson, P.; Smith, P.; Blake, A.; Stewart, D. Different polyphenolic components of soft fruits inhibit alpha-amylase and alpha-glucosidase. J. Agric. Food Chem. 2005, 53, 2760-2766.
13. Zhang, J.; Kashket, S. Inhibition of salivary amylase by black and green teas and their effects on the intraoral hydrolysis of starch. Caries Res. 1998, 32, 233-238.
14. He, Q.; Lv, Y.; Yao, K. Effects of tea polyphenols on the activities of α-amylase, pepsin, trypsin and lipase. Food Chem. 2006, 101, 1178-1182.
15. Tadera, K.; Minami, Y.; Takamatsu, K.; Matsuoka, T. Inhibition of alpha-glucosidase and alpha-amylase by flavonoids. J. Nutr. Sci. Vitaminol. 2006, 52, 149-153.
16. Rydberg, E. H.; Li, C.; Maurus, R.; Overall, C. M.; Brayer, G. D.; Withers, S. G. Mechanistic analyses of catalysis in human pancreatic alpha-amylase: detailed kinetic and structural studies of mutants of three conserved carboxylic acids. Biochemistry 2002, 41, 4492-4502.
17. O'Connor, C. M.; McGeeney, K. F. Interaction of human alpha-amylases with inhibitors from wheat flour. Biochim. Biophys. Acta 1981, 658, 397-405.
18. Marshall, J. J.; Lauda, C. M. Purification and properties of phaseolamin, an inhibitor of alpha-amylase, from the kidney bean, Phaseolus vulgaris. J. Biol. Chem. 1975, 250, 8030-8037.
19. Jia, W.; Gao, W.; Tang, L. Antidiabetic herbal drugs officially approved in China. Phytother. Res. 2003, 17, 1127-1134.
20. McCue, P.; Vattem, D.; Shetty, K. Inhibitory effect of clonal oregano extracts against porcine pancreatic amylase in vitro. Asia Pac. J. Clin. Nutr. 2004, 13, 401-408.
21. Starch blockers do not block starch digestion. Nutr. Rev. 1985, 43, 46-48.
22. Silano, V.; Furia, M.; Gianfreda, L.; Macri, A.; Palescandolo, R.; Rab, A.; Scardi, V.; Stella, E.; Valfre, F. Inhibition of amylases from different origins by albumins from the wheat kernel. Biochim. Biophys. Acta 1975, 391, 170-178.
23. O'Donnell, M. D.; McGeeney, K. F. Purification and properties of an alpha-amylase inhibitor from wheat. Biochim. Biophys. Acta 1976, 422, 159-169.
24. Marais, J. P.; De Wit, J. L.; Quicke, G. V. A critical examination of the Nelson-Somogyi method for the determination of reducing sugars. Anal. Biochem. 1966, 15, 373-381.
25. Guex, N.; Peitsch, M. C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 1997, 18, 2714-2723.
26. Maestro, version 7.5; Schrödinger LLC: Portland, OR, 2004.
27. Banks, J. L.; Beard, H. S.; Cao, Y.; Cho, A. E.; Damm, W.; Farid, R.; Felts, A. K.; Halgren, T. A.; Mainz, D. T.; Maple, J. R.; Murphy, R.; Philipp, D. M.; Repasky, M. P.; Zhang, L. Y.; Berne, B. J.; Friesner, R. A.; Gallicchio, E.; Levy, R. M. Integrated modeling program, applied chemical theory (IMPACT). J. Comput. Chem. 2005, 26, 1752-1780.
28. Halgren, T. A.; Murphy, R. B.; Friesner, R. A.; Beard, H. S.; Frye, L. L.; Pollard, W. T.; Banks, J. L. Glide: a new approach for rapid, accurate docking and scoring. 2. Enrichment factors in database screening. J. Med. Chem. 2004, 47, 1750-1759.
29. Friesner, R. A.; Banks, J. L.; Murphy, R. B.; Halgren, T. A.; Klicic, J. J.; Mainz, D. T.; Repasky, M. P.; Knoll, E. H.; Shelley, M.; Perry, J. K.; Shaw, D. E.; Francis, P.; Shenkin, P. S. Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy. J. Med. Chem. 2004, 47, 1739-1749.
30. Friesner, R. A.; Murphy, R. B.; Repasky, M. P.; Frye, L. L.; Greenwood, J. R.; Halgren, T. A.; Sanschagrin, P. C.; Mainz, D. T. Extra precision glide: docking and scoring incorporating a model of hydrophobic enclosure for protein-ligand complexes. J. Med. Chem. 2006, 49, 6177-6196.
31. McMartin, C.; Bohacek, R. S. QXP: powerful, rapid computer algorithms for structure-based drug design. J. Comput.-Aided Mol. Des. 1997, 11, 333-344.
32. Jorgensen, W. L.; Maxwell, D. S.; Tirado-Rives, J. Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids. J. Am. Chem. Soc. 1996, 118, 11225-11236.