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  • Title: Affinities of BO-2727 for bacterial penicillin-binding proteins and morphological change of gram-negative rods.
    Author: Hashizume T, Nakamura K, Nakagawa S.
    Journal: J Antibiot (Tokyo); 1997 Feb; 50(2):139-42. PubMed ID: 9099223.
    Abstract:
    Affinities of BO-2727, a new carbapenem, for penicillin-binding proteins (PBPs) of Escherichia coli. Pseudomonas aeruginosa and Staphylococcus aureus were studied. BO-2727 showed preferential affinity for PBP-2 of E. coli. and induced swollen and ovoid cells, when the organism was exposed to the MIC. In contrast, BO-2727 bound to both PBPs-2 and -3 of P. aeruginosa to a similar extent, and induced short filament cells with bulge. As compared with imipenem and meropenem, there was an observed difference in the affinity, especially for PBP-3, in both organisms; BO-2727 displayed intermediate affinity for PBP-3 between meropenem and imipenem. Studies on the affinity for PBPs of methicillin-susceptible S. aureus showed that the IC50 values for PBP-1 was roughly correlated with the MIC values of carbapenems tested, but those for the PBPs-2 and -3 appeared to be greater than the MIC values. In further studies on the affinity for PBP-2' of methicillin-resistant S. aureus. BO-2727 displayed better binding kinetics than imipenem, which reflected the better activity of BO-2727 than that of imipenem.
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