Syntheses and kinetic evaluation of hydroxamate-based peptide inhibitors of glyoxalase I

Bioorganic and Medicinal Chemistry Letters

Volumn 8, Issue 7, 1998, Pages 705-710

  Ly, Hoa D ^a   Clugston, Susan L ^a   Sampson, Peter B ^a   Honek, John F ^a  

^a UNIVERSITY OF WATERLOO   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME INHIBITOR; HYDROXAMIC ACID DERIVATIVE; LACTOYLGLUTATHIONE LYASE;

ANTIMICROBIAL ACTIVITY; ARTICLE; COMPETITIVE INHIBITION; DRUG ACTIVITY; DRUG SYNTHESIS; ENZYME INHIBITION; NONHUMAN; REACTION ANALYSIS; SACCHAROMYCES CEREVISIAE;

BINDING, COMPETITIVE; DRUG DESIGN; ENZYME INHIBITORS; HYDROXAMIC ACIDS; INDICATORS AND REAGENTS; KINETICS; LACTOYLGLUTATHIONE LYASE; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR STRUCTURE; OLIGOPEPTIDES; SACCHAROMYCES CEREVISIAE; SPECTROMETRY, MASS, FAST ATOM BOMBARDMENT;

SACCHAROMYCES CEREVISIAE;

EID: 0032492703     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-894X(98)00116-4     Document Type: Article

References (36)

1. 1. Vander Jagt, D. L. In Coenzymes and Cofactors VIII: Glutathione; Dolphin, D.; Poulsin, R.; Avramović, O. Eds.; Wiley: N.Y., 1989; Part A, pp 597-641.
2. 2. Thornalley, P. J. Crit. Rev. Oncol./Hematol. 1995, 20, 99.
3. 3. (a) Vander Jagt, D. L. J. Med. Chem. 1975, 18, 1155.
4. (b) Richard, J. P. Biochemistry 1991, 30, 4581.
5. 4. (a) Hooper, N. I.; Tisdale, M. J.; Thornalley, P. J. Leuk, Res. 1987, 11, 1141.
6. (b) Ayoub, F.; Zaman, M.; Thornalley, P.; Masters, J. Anticancer Res. 1993, 13, 151.
7. (c) Tew, K. D.; Monks, A.; Barone, L.; Rosser, D.; Akerman, G.; Montali, J. A.; Wheatley, J. B.; Schmidt, D. E. Jr. Mol. Pharmacol. 1996, 50, 149.
8. 5. (a)Vince, R.; Daluge, S.; Wadd, W. B. J. Med. Chem. 1971, 14, 402.
9. (b) Jordan, F.; Cohen, J. F.; Wang, C.-T.; Wilmott, J. M.; Hall, S. S. Drug Metab. Rev. 1983, 14, 723.
10. (c) Thornalley, P. J.; Ladan, M. J.; Ridgway, S. J. S.; Kang, Y. J. Med. Chem. 1996, 39, 3409.
11. 6. (a) Douglas, K. T.; Gohel, D. I.; Nadvi, I. N.; Quilter, A. J.; Seddon, A. P. Biochim. Biophys. Acta 1985, 829, 109.
12. (b) Barnard, J. F.; Honek, J. F. Biochem. Biophys. Res. Commun. 1989, 165, 118.
13. 7. (a) Hamilton, D. S.; Creighton, D. J. J. Biol. Chem. 1992, 267, 24933.
14. (b) Murthy, N. S. R. K.; Bakeris, T.; Kavarana, M. J.; Hamilton, D. S.; Lan, Y.; Creighton, D. J. J. Med. Chem. 1994, 37, 2161.
15. 8. (a) Barnard, J. F.; Vander Jagt, D. L.; Honek, J. F. Biochim. Biophys. Acta 1994, 1208, 127.
16. (b) Clugston, S. L.; Daub, E.; Kinach, R.; Miedema, D.; Barnard, J. F. J.; Honek, J. F. Gene 1997, 186, 103.
17. 9. (a) Davenport, R. C.; Bash, P. A.; Seaton, B. A.; Karplus, M.; Petsko, G. A.; Ringe, D. Biochemistry 1991, 30, 5821.
18. (b) Verlinde, C. L. M. J.; Witmans, C. J.; Pijning, T.; Kalk, K. H.; Hol, W. G. J.; Callens, M.; Opperdoes, F. R. Protein Sci. 1992, 1, 1578.
19. 10. Anderson, M. E.; Powrie, F.; Puri, R. N.; Meister, A. Arch. Biochem. Biophys. 1985, 239, 538.
20. 11. Dourtoglou, V.; Gross B. Synthesis 1984, 572.
21. 12. Anwer, M. K.; Spatola, A. F. Synthesis 1980, 929.
22. 13. Sulsky, R.; Demers, J. P. Tetrahedron Lett. 1989, 30, 31.
23. 3); m/z (FABMS) 363.1515 (M+1, 100%).
24. 7a Inhibitors 8a,b and 9a,b were dissolved in water and 10 in DMSO (final volume of DMSO of 1% (v/v) in the GIxI assays, which did not affect the GIxI enzymatic activity). Non-linear regression analysis and F-tests were utilized.
25. 16. Hamilton, D. S.; Creighton, D. J. Biochim. Biophys. Acta 1992, 1159, 203.
26. 17. Collins, K. D. J. Biol. Chem. 1974, 249, 136.
27. 18. Marmstål, E.; Mannervik, B. FEBS Lett. 1979, 102, 162.
28. 19. Cameron, A. D.; Olin, B.; Ridderström, M.; Mannervik, B.; Jones, T. A. EMBO J. 1997, 16, 3386.
29. 20. Calculations performed utilizing PC SPARTAN (Wavefunction Inc., Irvine CA) or Gaussian 94, Rev. C.3 (Gaussian, Inc., Pittsburgh PA). CHe1pG is based on Breneman, C. M.; Wiberg, K. B. J. Comp. Chem. 1990, 11, 361.
30. 2O, pD 7.0 was utilized. The solutions were monitored at 23 °C for 4 days (N-methyl protons), and the enzyme activity monitored at intervals. Electrospray mass spectrometry data were collected on a Micromass Quattro II triple-stage quadrupole mass spectrometer. Two units of GIxII and 5 mM 9b were dissolved to a total volume of 50 μL in 100 mM Tris-HCl, pH 7.4. The reaction was monitored at intervals over a 24 h period. NMR and mass spectral analysis indicated that 9b is not hydrolyzed by bovine liver GIxII.
31. 22. Inhibition of bovine liver GIxII by 9b was studied by measuring the activity of the enzyme at inhibitor concentrations of 100 μM-1.5 mM. Studies were performed with 0.5 mM S-lactoylglutathione, 0.1 units of enzyme/mL, in 100 mM potassium phosphate buffer, pH 7.4, 25 °C. The decrease in the absorbance of the substrate was monitored at 240 nm for 90 seconds and the initial velocity determined from the slope.
32. 23. (a) Anticancer testing at NCl was based on the method of Boyd, M. R.; Paull, K. D. Drug Dev. Res. 1995, 34, 91.
33. 50 values against the D6 and W2 strains of P. falciparum are 30 nM and 142 nM, respectively.
34. 24. Powers, J. C.; Harper, J. W. In Proteinase Inhibitors; Barrett, A. J.; Salvensen, G., Eds; Elsevier: New York, 1986; pp 219-298.
35. 25. (a) Bergmeyer, H. U.; Graßl, M.; Walter, H.-E. In Methods of Enzymatic Analysis; Bergmeyer, H. U. Ed.; Verlag Chemie: Deerfield Beach, Florida, 1983; Vol. 2, pp 217-218.
36. (b) Vander Jagt, D. L.; Han, L.-P. B.; Lehman, C. H. Biochemistry 1972, 11, 3735.