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Volumn 13, Issue 13, 2003, Pages 2109-2112

Structural features of piperazinyl-linked ciprofloxacin dimers required for activity against drug-resistant strains of Staphylococcus aureus

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; CIPROFLOXACIN; DIMER; DNA TOPOISOMERASE IV; MONOMER; PIPEMIDIC ACID; PIPERAZINE DERIVATIVE; QUINOLINE DERIVED ANTIINFECTIVE AGENT;

EID: 0037534121     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-894X(03)00376-7     Document Type: Article
Times cited : (95)

References (13)
  • 6
    • 85031175935 scopus 로고    scopus 로고
    • 1H NMR and mass spectroscopic analysis.
  • 7
    • 85031167399 scopus 로고    scopus 로고
    • 2.
  • 8
    • 85031174308 scopus 로고    scopus 로고
    • MICs were determined by broth microdilution following NCCLS guidelines using 2-fold dilutions of test compound. Error for MICs is therefore±one dilution.
  • 11
    • 85031175208 scopus 로고    scopus 로고
    • We have previously shown that symmetric fluoroquinolone dimers do not interfere with NorA-mediated efflux of ethidium bromide in SA 1199-B at concentrations up to five times the MIC and are not competitive substrates for this pump. Therefore it is likely that the incomplete dimers here similarly are not substrates for the NorA pump, accounting for their ability to evade this efflux mechanism.
  • 12
    • 0026045096 scopus 로고
    • (a) The primary target of ciprofloxacin in S. aureus is topoisomerase IV. One explanation for the observed activity against SA 1199B is that the primary target of the dimers has switched from topoisomerase IV to DNA gyrase. Investigations are underway to determine target selectivity of the piperazinyl-linked fluoroquinolone dimers.
    • (a) The primary target of ciprofloxacin in S. aureus is topoisomerase IV. One explanation for the observed activity against SA 1199B is that the primary target of the dimers has switched from topoisomerase IV to DNA gyrase. Investigations are underway to determine target selectivity of the piperazinyl-linked fluoroquinolone dimers. (b) . Previous reports of other fluoroquinolone analogues having varied substitutents at the C-7 position have shown that hydrophobic or bulky substituents at this position often result in analogues that are not substrates for the NorA efflux pump system. Piddock L.J.V., Zhu M. Antimicrob. Agents Chemother. 35:1991;2423 Takenouchi T., Tabata F., Iwata Y., Hanzawa H., Sugawara M., Ohya S. Antimicrob. Agents Chemother. 40:1996;1835.
    • (1991) Antimicrob. Agents Chemother. , vol.35 , pp. 2423
    • Piddock, L.J.V.1    Zhu, M.2
  • 13
    • 0029849429 scopus 로고    scopus 로고
    • Previous reports of other fluoroquinolone analogues having varied substitutents at the C-7 position have shown that hydrophobic or bulky substituents at this position often result in analogues that are not substrates for the NorA efflux pump system.
    • (a) The primary target of ciprofloxacin in S. aureus is topoisomerase IV. One explanation for the observed activity against SA 1199B is that the primary target of the dimers has switched from topoisomerase IV to DNA gyrase. Investigations are underway to determine target selectivity of the piperazinyl-linked fluoroquinolone dimers. (b) . Previous reports of other fluoroquinolone analogues having varied substitutents at the C-7 position have shown that hydrophobic or bulky substituents at this position often result in analogues that are not substrates for the NorA efflux pump system. Piddock L.J.V., Zhu M. Antimicrob. Agents Chemother. 35:1991;2423 Takenouchi T., Tabata F., Iwata Y., Hanzawa H., Sugawara M., Ohya S. Antimicrob. Agents Chemother. 40:1996;1835.
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 1835
    • Takenouchi, T.1    Tabata, F.2    Iwata, Y.3    Hanzawa, H.4    Sugawara, M.5    Ohya, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.