Design, synthesis, and evaluation of 2β-alkenyl penam sulfone acids as inhibitors of β-lactamases

Journal of Medicinal Chemistry

Volumn 39, Issue 19, 1996, Pages 3712-3722

  Richter, Hans G F ^a   Angehrn, Peter ^a   Hubschwerlen, Christian ^a   Kania, Malgosia ^a   Page, Malcolm G P ^a   Specklin, Jean Luc ^a   Winkler, Fritz K ^a  

^a F HOFFMANN LA ROCHE LTD   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

BETA LACTAMASE; CEPHALOSPORINASE; PENAM DERIVATIVE; SULBACTAM;

ANTIBIOTIC RESISTANCE; ARTICLE; BINDING AFFINITY; CHEMICAL ANALYSIS; CITROBACTER FREUNDII; DRUG SYNTHESIS; ENZYME ACTIVITY; ENZYME INHIBITION; PSEUDOMONAS AERUGINOSA; RECEPTOR BINDING; ULTRAVIOLET RADIATION; X RAY CRYSTALLOGRAPHY;

BETA-LACTAMASES; BETA-LACTAMS; CEFTRIAXONE; CITROBACTER FREUNDII; CLAVULANIC ACID; CLAVULANIC ACIDS; CRYSTALLOGRAPHY, X-RAY; DRUG DESIGN; DRUG SYNERGISM; ENTEROBACTER; ENZYME INHIBITORS; LACTAMS; MODELS, MOLECULAR; MOLECULAR STRUCTURE; PSEUDOMONAS; SPECTROPHOTOMETRY, ULTRAVIOLET;

EID: 0029795726     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm9601967     Document Type: Article

References (34)

1. Neu, H. C. The Crisis in Antibiotic Resistance. Science 1992, 257, 1064-1072.
2. Ambler, R. P. The Structure of β-Lactamases. Philos. Trans. R. Soc. London Ser. B 1980, 289, 321-331.
3. Sanders, C. C.; Sanders, W. E. J. β-Lactam Resistance in Gram-negative Bacteria: Global Trends and Clinical Impact. Clin. Infect. Dis. 1992, 15, 824-839.
4. Pratt, R. F. β-Lactamase Inhibition. In The Chemistry of β-Lactams; Page, M. I., Ed.; Blackie Academic & Professional: Glascow, 1992; pp 229-271.
5. Livermore, D. M. Determinants of the Activity of β-Lactamase Inhibitor Combinations. J. Antimicrob. Chemother. 1993, 31 (Suppl. A), 9-21.
6. Bush, K.; Macalintal, C.; Rasmussen, B. A.; Lee, V. J.; Yang, Y. Kinetic Interactions of Tazobactam with β-Lactamases from All Major Structural Classes. Antimicrob. Agents Chemother. 1993, 37, 851-858.
7. Moews, P. C.; Knox, J. R.; Dideberg, O.; Charlier, P.; Frère, J.-M. β-Lactamase of Bacillus licheniformis 749/C at 2Å Resolution. PROTEINS: Struct. Funct. Genet. 1990, 7, 156-171.
8. Oefner, C.; D'Arcy, A.; Daly, J. J.; Gubernator, K.; Charnas, R. L.; Heinze, I.; Hubschwerlen, C.; Winkler, F. K. Refined Crystal Structure of β-Lactamase from Citrobacter freundii Indicates a Mechanism for β-Lactam Hydrolysis. Nature 1990, 343, 284-288.
9. Lobkovsky, E.; Moews, P. C.; Lin, H.; Zhao, H.; Frère, J.-M.; Knox, J. R. Evolution of an Enzyme Activity: Crystallographic Structure at 2-Å Resolution of a Cephalosporinase from the ampC Gene of Enterobacter cloacae P99 and Comparison with a Class A Penicillinase. Proc. Natl Acad. Svi. U.S.A. 1993, 90, 11257-11261.
10. Strynadka, N. C. J.; Adachi, H.; Jensen, S. E.; Johns, K.; Sielecki, A.; Betzel, C.; Sutoh, K.; James, M. N. G. Molecular Structure of the Acyl-enzyme Intermediate in β-Lactam Hydrolysis at 1.7Å Resolution. Nature 1992, 359, 700-705.
11. Jelsch, C.; Mourey, L.; Masson, J.-M.; Samama, J.-P. Crystal Structure of Escherichia coli TEM-1 β-Lactamase at 1.8Å Resolution. PROTEINS: Struct., Funct. Genet. 1993, 16, 364-383.
12. Toomer, C. T.; Schwalbe, C. H.; Ringan, N. S.; Lambert, P. A.; Lowe, P. R.; Lee, V. J. Structural Studies on Tazobactam. J. Med. Chem. 1991, 34, 1944-1947.
13. Imtiaz, U.; Billings, E. M.; Knox, J. R.; Mobashery, S. A Structure-Based Analysis of the Inhibition of Class A β-Lactamases by Sulbactam. Biochemistry 1994, 33, 5728-5738.
14. Brenner, D. G.; Knowles, J. R. Penicillanic Acid Sulfone: An Unexpected Isotope Effect in the Interaction of 6α- and 6β-Monodeuterio and of 6,6-Dideuterio Derivatives with RTEM β-Lactamase from Escherichia coli. Biochemistry 1981, 20, 3680-3687.
15. Chen, C. C. H.; Herzberg, O. Inhibition of β-Lactamase by Clavulanate. Trapped Intermediates in Cryocrystallographic Studies. J. Mol. Biol. 1992, 224, 1103-1113.
16. Micetich, R. G.; Maiti, S. N.; Spevak, P.; Tanaka, M.; Yamazaki, T.; Ogawa, K. Synthesis of 2β-Azidomethylpenicillin-1,1-dioxides and 3β-Azido-3α-methylcepham-1,1-dioxides. Synthesis 1986, 292-296.
17. Chern, J.-W.; Huang, M.; Tien, J.-H.; Pai, S.-H. Efficient Preparation of Penicillanate Ester: A Reductive Debromination of Bromopenicillanate Ester and Bromopenicillanate-S,S-dioxide Ester with Tri-n-butylphosphine. Heterocycles 1988, 27, 1349-1351.
18. Kamiya, T.; Teraji, T.; Saito, Y.; Hashimoto, M.; Nakaguchi, O.; Oku, T. Studies on β-Lactam Antibiotics. I. A Novel Conversion of Penicillins into Cephalosporins. Tetrahedron Lett. 1973, 32, 3001-3004.
19. Baldwin, J. E.; Cobb, J. E.; Sheppard, L. N. Functionalization of the 3β-Methyl Group of Penicillin. Tetrahedron 1987, 43, 1003-1012.
20. Tidwell, T. T. Oxidation of Alcohols by Activated Dimethyl Sulfoxide and Related Reactions: An Update. Synthesis 1990, 857-870.
21. Fass, R. J.; Prior, R. B. Comparative In Vitro Activities of Piperacillin-Tazobactam and Ticarcillin-Clavulanate. Antimicrob. Agents Chemother. 1989, 33, 1268-1274.
22. Kemal, C.; Knowles, J. R. Penicillanic Acid Sulfone: Interaction with RTEM β-Lactamase from Escherichia coli at Different pH Values. Biochemistry 1980, 20, 3688-3695.
23. Claisse, J. A.; Foxton, M. W.; Gregory, G. I.; Sheppard, A. H.; Tiley, E. P.; Warburton, W. K.; Wilson, M. J. 5-Unsubstituted Acetylenic and Vinylic 1,2,4-Oxadiazoles. J. Chem. Soc., Perkin Trans. 1 1973, 20, 2241-2249.
24. Bruenger, A. T.; Kuriyan, J.; Karplus, M. Crystallographic R Factor Refinement by Molecular Dynamics. Science 1987, 235, 458-460.
25. Bruenger, A. T. The R value: a Novel Statistical Quantity for Assessing the Accuracy of Crystal Structures. Nature 1992, 355, 472-475.
26. Kabsch, W. Evaluation of Single-Crystal X-ray Diffraction Data from a Position-Sensitive Detector. J. Appl. Crystallogr. 1988, 21, 916-924.
27. Gerber, P. R.; Müller, K. MAB: a Generally Applicable Molecular Force Field for Structure Modelling in Medicinal Chemistry. J. Comput.-Aided Mol. Des. 1995, in press.
28. Page, M. G. P. The Kinetics of Non-stoichiometric Bursts of β-Lactam Hydrolysis Catalysed by Class C β-Lactamases. Biochem. J. 1993, 295, 295-304.
29. Dubus, A.; Normark, S.; Kania, M.; Page, M. G. P. The Role of Tyrosine 150 in Catalysis of β-Lactam Hydrolysis by AmpC β-Lactamase from Escherichia coli Investigated by Site-directed Mutagenesis. Biochemistry 1994, 33, 8577-8586.
30. Then, R. L.; Kohl, I. Affinity of Carumonam for Penicillin-binding Proteins. Chemotherapy 1985, 31, 246-254.
31. Laible, G.; Hakenbeck, R.; Sicard, M. A.; Joris, B.; Ghuysen, J.-M. Nucleotide sequences of the pbpx genes encoding the penicillin-binding proteins 2x from Streptococcus pneumoniae R6 and a cefotaxime-resistant mutant, C506. Mol. Microbiol. 1989, 3, 1337-1348.
32. Laible, G.; Hakenbeck, R. Five Independent Combinations of Mutations Can Result in Low-Affinity Penicillin-Binding Protein 2x of Streptococcus pneumoniae. J. Bacteriol. 1991, 173, 6986-6990.
33. Bush, K. Classification of β-Lactamases: Groups 1, 2a, 2b and 2b′. Antimicrob. Agents Chemother. 1989, 33, 264-270; Bush, K. Classification of β-Lactamases: Groups 2c, 2d, 2e, 3 and 4. Antimicrob. Agents Chemother. 1989, 33, 271-276.
34. Bush, K. Classification of β-Lactamases: Groups 1, 2a, 2b and 2b′. Antimicrob. Agents Chemother. 1989, 33, 264-270; Bush, K. Classification of β-Lactamases: Groups 2c, 2d, 2e, 3 and 4. Antimicrob. Agents Chemother. 1989, 33, 271-276.