De novo design of α-amylase inhibitor: A small linear mimetic of macromolecular proteinaceous ligands

Chemistry and Biology

Volumn 12, Issue 12, 2005, Pages 1349-1357

  Dolečková Marešová, Lucie ^a   Pavlík, Manfred ^a   Horn, Martin ^a   Mareš, Michael ^a  

^a INSTITUTE OF ORGANIC CHEMISTRY AND BIOCHEMISTRY   (Czech Republic)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLASE; ENZYME INHIBITOR; LIGAND; PEPTIDE LIBRARY;

ANIMAL; ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; DRUG ANTAGONISM; KINETICS; MOLECULAR MIMICRY; PROTEIN MOTIF; SWINE;

ALPHA-AMYLASE; AMINO ACID MOTIFS; ANIMALS; BINDING SITES; ENZYME INHIBITORS; KINETICS; LIGANDS; MOLECULAR MIMICRY; MOLECULAR STRUCTURE; PEPTIDE LIBRARY; SWINE;

SUIDAE;

EID: 28844504697     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2005.10.005     Document Type: Article

References (37)

1. H.W. Breuer Review of acarbose therapeutic strategies in the long-term treatment and in the prevention of type 2 diabetes Int. J. Clin. Pharmacol. Ther. 41 2003 421 440
2. O.L. Franco, D.J. Rigden, F.R. Melo, and M.F. Grossi-De-Sa Plant α-amylase inhibitors and their interaction with insect α-amylases Eur. J. Biochem. 269 2002 397 412
3. E. Truscheit, W. Frommer, B. Junge, L. Müller, D.D. Schmidt, and W. Wingender Chemistry and biochemistry of microbial α-glucosidase inhibitors Angew. Chem. Int. 20 1981 744 761
4. B. Svensson, K. Fukuda, P.K. Nielsen, and B.C. Bonsager Proteinaceous α-amylase inhibitors Biochim. Biophys. Acta 1696 2004 145 156
5. C. Bompard-Gilles, P. Rousseau, P. Rouge, and F. Payan Substrate mimicry in the active center of a mammalian α-amylase: structural analysis of an enzyme-inhibitor complex Structure 4 1996 1441 1452
6. G. Wiegand, O. Epp, and R. Huber The crystal structure of porcine pancreatic α-amylase in complex with the microbial inhibitor Tendamistat J. Mol. Biol. 247 1995 99 110
7. P.J. Pereira, V. Lozanov, A. Patthy, R. Huber, W. Bode, S. Pongor, and S. Strobl Specific inhibition of insect α-amylases: yellow meal worm α-amylase in complex with the amaranth α-amylase inhibitor at 2.0 Å resolution Structure 7 1999 1079 1088
8. F. Vallee, A. Kadziola, Y. Bourne, M. Juy, K.W. Rodenburg, B. Svensson, and R. Haser Barley α-amylase bound to its endogenous protein inhibitor BASI: crystal structure of the complex at 1.9 Å resolution Structure 6 1998 649 659
9. S. Strobl, K. Maskos, G. Wiegand, R. Huber, F.X. Gomis-Ruth, and R. Glockshuber A novel strategy for inhibition of α-amylases: yellow meal worm α-amylase in complex with the Ragi bifunctional inhibitor at 2.5 Å resolution Structure 6 1998 911 921
10. J. Lehtio, T.T. Teeri, and P.A. Nygren α-amylase inhibitors selected from a combinatorial library of a cellulose binding domain scaffold Proteins 41 2000 316 322
11. A. Desmyter, S. Spinelli, F. Payan, M. Lauwereys, L. Wyns, S. Muyldermans, and C. Cambillau Three camelid VHH domains in complex with porcine pancreatic α-amylase. Inhibition and versatility of binding topology J. Biol. Chem. 277 2002 23645 23650
12. H. Matter, and H. Kessler Structures, dynamics, and biological activities of 15 cyclic hexapeptide analogs of the α-amylase inhibitor Tendamistat (HOE 467) in solution J. Am. Chem. Soc. 117 1995 3347 3359
13. H. Baumann, S. Ohrman, Y. Shinohara, O. Ersoy, D. Choudhury, A. Axen, U. Tedebark, and E. Carredano Rational design, synthesis, and verification of affinity ligands to a protein surface cleft Protein Sci. 12 2003 784 793
14. Coutinho, P.M., and Henrissat, B. (1999). Carbohydrate-Active Enzymes Server at URL (http://afmb.cnrs-mrs.fr/CAZY/ ).
15. R. Koukiekolo, V. Le Berre-Anton, V. Desseaux, Y. Moreau, P. Rouge, G. Marchis-Mouren, and M. Santimone Mechanism of porcine pancreatic α-amylase inhibition of amylose and maltopentaose hydrolysis by kidney bean (Phaseolus vulgaris) inhibitor and comparison with that by acarbose Eur. J. Biochem. 265 1999 20 26
16. M. Al Kazaz, V. Desseaux, G. Marchis-Mouren, E. Prodanov, and M. Santimone The mechanism of porcine pancreatic α-amylase. Inhibition of maltopentaose hydrolysis by acarbose, maltose and maltotriose Eur. J. Biochem. 252 1998 100 107
17. M. Qian, R. Haser, G. Buisson, E. Duee, and F. Payan The active center of a mammalian α-amylase. Structure of the complex of a pancreatic α-amylase with a carbohydrate inhibitor refined to 2.2-Å resolution Biochemistry 33 1994 6284 6294
18. J.R. Powers, and J.R. Whitaker Effect of several experimental parameters on combination of red kidney bean (Phaseolus vulgaris) α-amylase inhibitor with porcine pancreatic α-amylase J. Food Biochem. 1 1977 239 260
19. M.H. Roehrl, J.Y. Wang, and G. Wagner A general framework for development and data analysis of competitive high-throughput screens for small-molecule inhibitors of protein-protein interactions by fluorescence polarization Biochemistry 43 2004 16056 16066
20. G. Ferey-Roux, J. Perrier, E. Forest, G. Marchis-Mouren, A. Puigserver, and M. Santimone The human pancreatic α-amylase isoforms: isolation, structural studies and kinetics of inhibition by acarbose Biochim. Biophys. Acta 1388 1998 10 20
21. A.M. Sefler, M.C. Kozlowski, T. Guo, and P.A. Bartlett Design, synthesis, and evaluation of a depsipeptide mimic of tendamistat J. Org. Chem. 62 1997 93 102
22. L. Kandra, A. Zajacz, J. Remenyik, and G. Gyemant Kinetic investigation of a new inhibitor for human salivary α-amylase Biochem. Biophys. Res. Commun. 334 2005 824 828
23. T.M. Gloster, J.M. Macdonald, C.A. Tarling, R.V. Stick, S.G. Withers, and G.J. Davies Structural, thermodynamic, and kinetic analyses of tetrahydrooxazine-derived inhibitors bound to β-glucosidases J. Biol. Chem. 279 2004 49236 49242
24. D.L. Zechel, A.B. Boraston, T. Gloster, C.M. Boraston, J.M. Macdonald, D.M. Tilbrook, R.V. Stick, and G.J. Davies Iminosugar glycosidase inhibitors: structural and thermodynamic dissection of the binding of isofagomine and 1-deoxynojirimycin to β-glucosidases J. Am. Chem. Soc. 125 2003 14313 14323
25. A. Solovicova, T. Christensen, E. Hostinova, J. Gasperik, J. Sevcik, and B. Svensson Structure-function relationships in glucoamylases encoded by variant Saccharomycopsis fibuligera genes Eur. J. Biochem. 264 1999 756 764
26. D.R. Houston, K. Shiomi, N. Arai, S. Omura, M.G. Peter, A. Turberg, B. Synstad, V.G. Eijsink, and D.M. van Aalten High-resolution structures of a chitinase complexed with natural product cyclopentapeptide inhibitors: mimicry of carbohydrate substrate Proc. Natl. Acad. Sci. USA 99 2002 9127 9132
27. I. Kluh, M. Horn, J. Hyblova, J. Hubert, L. Doleckova-Maresova, Z. Voburka, I. Kudlikova, F. Kocourek, and M. Mares Inhibitory specificity and insecticidal selectivity of α-amylase inhibitor from Phaseolus vulgaris Phytochemistry 66 2005 31 39
28. J. Eichler, and R.A. Houghten Identification of substrate-analog trypsin inhibitors through the screening of synthetic peptide combinatorial libraries Biochemistry 32 1993 11035 11041
29. C. Pinilla, J. Appel, S. Blondelle, C. Dooley, B. Dorner, J. Eichler, J. Ostresh, and R.A. Houghten A review of the utility of soluble peptide combinatorial libraries Biopolymers 37 1995 221 240
30. E. Atherton, and R.C. Sheppard Solid Phase Peptide Synthesis: A Practical Approach 1989 IRL Press at Oxford University Press Oxford, UK
31. B. Kamber, A. Hartmann, K. Eisler, B. Riniker, H. Rink, P. Sieber, and W. Rittel The synthesis of cystine peptides by iodine oxidation of S-trityl-cysteine and S-acetamidomethyl-cysteine peptides Hevl. Chim. Acta 63 1980 899 915
32. E. Rauscher, U. Neumann, E. Schaich, S. von Bulow, and A.W. Wahlefeld Optimized conditions for determining activity concentration of α-amylase in serum, with 1,4-α-D-4-nitrophenylmaltoheptaoside as substrate Clin. Chem. 31 1985 14 19
33. M. Horn, M. Pavlik, L. Doleckova, M. Baudys, and M. Mares Arginine-based structures are specific inhibitors of cathepsin C. Application of peptide combinatorial libraries Eur. J. Biochem. 267 2000 3330 3336
34. J.R. Lakowicz Principles of Fluorescence Spectroscopy 1999 Plenum New York
35. M.M. Pierce, C.S. Raman, and B.T. Nall Isothermal titration calorimetry of protein-protein interactions Methods 19 1999 213 221
36. H. Fukada, and K. Takahashi Enthalpy and heat capacity changes for the proton dissociation of various buffer components in 0.1 M potassium chloride Proteins 33 1998 159 166
37. R.B. Raffa, G.W. Stagliano, and S.D. Spencer Protonation effect on drug affinity Eur. J. Pharmacol. 483 2004 323 324