Comparison of the Activities of Novel ${\beta}$-Lactamase Inhibitors, 6-Exomethylene Penamsulfones, with Other ${\beta}$-Lactamase Inhibitors as Combined with ${\beta}$-Lactam Antibiotics (I)

6위치 엑소 메칠렌 치환 페남계 베타락타마제 억제제의 베타락탐항생제와 병용시 활성비교(I)

  • Published : 1997.08.01

Abstract

In this approach, the antimicrobial activities of the compounds were compared with the ${\beta}$-lactam antibiotics against ${\beta}$-lactamase producing strains in vitro. Heteroc yclyl exomethylenepenam derivatives were several numbers of 6-exomethylenepenam sodiums (CH1240, CH1245, CH1250, CH2140, CH2145, CH2150). The inhibitory concentraion assay of six compounds were compared with clavulanic acid, sulbactam, tazobactam. Clavulanic acid, sulbactam and tazobactam are used as inhibitors of a variety of plasmid-mediated beta-lactamases. In vitro ${\beta}$-lactamase inhibitory assay, CH1240 and CH2140 were more active than clavulanic acid, sulbactam and tazobactam against ${\beta}$-lactamases overally. And in vitro comparative antimicrobial susceptibility test of six inhibitors were performed with mixed forms of ampicillin, cefotaxime, amoxicillin, ticarcillin, piperacillin, cefoperazone against ${\beta}$-lactamase producing 31 species strains. Consequently CH2140 and CH1240 among the six compounds enhanced the activity of the ${\beta}$-lactams for 31 ${\beta}$-lactamase producing strains.

Keywords

References

  1. Progress in Drug Research v.41 Bacterial resistance to β-lactam antiobiotics: problems and solutions Sutherland, R.;Ernst Jucker(ed.)
  2. J. Antimicrob. Chemother v.31 Activity of 13 β-lactam agents combined with BRL 42715 against β-lactamase producing Gram-negative bacteria compared to combinations with clavulanic acid, tazobactam and sulbactam Laura, J.V.;Piddoc;Yu Fang Jin;Turner, H.L.
  3. J. Antimicrob. Chemother v.31 no.(Suppl. A.) Determination of the activity if β-lactamase inhibitor combinations Livermore, D.M.
  4. J. Antiobiotics v.47 Synthesis and β-lactamase iinhibitory activity of 6-[(1-heteroarylthioethyl-1,2,3,-triazol-4-yl)-methtlene]penam sulfones Im, C.;Maiti, S.N.;Micetich, R.G.;Daneshtalab, M.;Tchison, K.;Phillips, O.A.;Kunugpia, C.
  5. J. Antimicrob. Chemother. v.31 no.Suppl. A. Meeting the challenges of β-lactamase Moellering, R.C.
  6. J. Pharm. Pharmac. v.21 Bacterial resistance to penicillins and cephalosporins Smith, J.T.;Hamilton-Miller, J.M.T.;Knox, R.
  7. J. BActeriol. v.153 Porin channels in E. coli: Studies with β-lactams in intact cells Nikaido, H.;Rosenberg, E.Y.;Foulds, J.
  8. Eur. J. Clin. Microbiol. Infect. Dis. v.13 no.Suppl. 1 Clinical significance of extended spectrum beta-lactamase Quinn, J.P.
  9. J. Antiobiotics v.44 6-(Substituted methtlene)penems. potent broad spectrum inhibitors of bacterial β-lactamase Bennet, I.;Broom, N.J.P.;Bruton, G.S.;Albert, C.;Clarke, B.P.;Coleman, K.;Edmondson, R.;Edwards, P.;Jones, D.;Osbone, N.F.;Walker, G.
  10. J. Antiobiotics v.43 6-(Substituted methylene)penems. potent broad spectrum inhibitors of bacterial β-lactamase Broom, N.J.P.;Coleman, K.;Hunter, P.A.;Osborne, N.F.
  11. Biochem. J. v.253 Imipenem as substrate and inhibitor of β-lactamase Monks, J.;Waley, G.S.
  12. Antimicrob. Agents Chemother v.33 Comparative in vitro activities of piperacillin-tazobactam and ticarcillian-clavulanate Fassand, J.R.;Prior, B.R.
  13. Pharmacotherapy v.11 Effects of β-lactamase-mediated antimicrobial resistance: The role of β-lactamase inhibitors Maddux, S.M.
  14. J. Antimicrob. Chemother v.27 Susceptibility of E. coli isolates with TEM-1 β-lactamase to combinations of BRL42715 tazobactam or clavulanate with piperacillin or amoxcillian Livermore, D.M.;Seetulsingh, P.
  15. Drugs v.35 no.suppl. 7 In vitro evaluations of amino penicillin/β-lactamase combination Jones, R.N.
  16. Drugs v.35 no.Suppl. 7 Sulbactam and clavulanic acid : Study with ampicillin and mezlocillin Cullamnn, W.;Stieglitz, M.;Opferkuch, W.
  17. Rev. Infec. Dis. v.8 no.Suppl. 5 Induction/inhibition of chromosomal β-lactamase by β-lactamase inhibitors Moosdeen, F.;Keeble, J.;Wiliiams, J.D.
  18. Clinic. Microb. Rev. v.1 β-lactamase Inhibitors from laboratory to clinic Bush, K.
  19. Biochem. J. v.251 β-Lactamase inhibitors Crompton, I.E.;Cuthbert, B.K;Lowe, G.;Waley, S.G.
  20. J. Antimicrob. Chemother v.22 The effect of clavulanic acid and sulbactam on β-lactamase biosynthesis Farmer, T.H.;Reading, C.
  21. J. Antimicrob. Chemother. v.26 comparative activities of the β-lactamase inhibitors YTR830, sodium clavulanate, and sulbactam combined with amoxicillin or ampicillin Aronoff, S.C.;Jacobs, M.R.;Johenning, S.;Yamabe, S.
  22. Rev. Infec. Dis. v.5 Emergence of resistance during therapy with the newer β-lactam antiobiotics Sanders, C.C.;Sanders, W.E.
  23. J. Antibiot. v.40 Structure activity relationships of 6-(heterocyclyl)-methylene penam sulfomes: a new class of β-lactamase inhibitors Chen, L.Y.;Chang, C.;Hederg, K.;Guarino, K.;Welch, W.M.;Kiessling, L.;Retema, H.;L. Suznne;Margaret, A.;Mary, M.;John, B.F.
  24. Antibiotic inactivating enzymes and bacterial resistance, antibiotics in Laboratory Medicine(2nd) Victor, L.(ed.)
  25. Proceedings of the International Symposium(13th Feb. 1986) BRL28500, biochemical and microbiological basis for therapy, BRL28500 Comber, K.R.
  26. Drugs of the Future v.6 Inhibitors of bacterial β-lactamase Cole, M.
  27. J. Antimicrob. Chemother. v.32 A guide to sensitivity testing Phillips, I.
  28. NCCLS Document M7-A2 v.10 Methods for Dilution Antimicrobial Susceptibility Tests for Bacteria thar Grow Aerobically(2nd) American national standards institute
  29. New End. J. Med. v.324 New mechanisms of bacterial resistance to antimicrobial agents Jacoby, G.A.;Archer, G.L.