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Cefonicid: a stable beta-lactamase inhibitor

R J Mehta, D J Newman, B A Bowie

    The Journal of Antibiotics
    |February 1, 1981
    PubMed
    Summary

    Cefonicid demonstrates significant stability against major beta-lactamase classes, offering improved resistance compared to cefamandole. It also acts as a non-competitive inhibitor of cephalothin hydrolysis by Type I beta-lactamase.

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    Area of Science:

    • Microbiology
    • Pharmacology
    • Enzymology

    Background:

    • Beta-lactamase enzymes are a primary mechanism of bacterial resistance to beta-lactam antibiotics.
    • Understanding antibiotic stability against various beta-lactamase classes is crucial for developing effective antimicrobial therapies.
    • Cefonicid is a cephalosporin antibiotic with potential clinical applications.

    Purpose of the Study:

    • To evaluate the stability of cefonicid against a panel of representative beta-lactamase enzymes.
    • To compare the stability of cefonicid with cefamandole against specific beta-lactamase types.
    • To investigate the inhibitory potential of cefonicid against beta-lactamase activity.

    Main Methods:

    • Spectrophotometric assays were employed to quantify the hydrolysis of cefonicid by beta-lactamase enzymes.
    • Enzymes tested included representatives from six major classes of beta-lactamases.
    • Kinetic parameters, including the inhibition constant (Ki), were determined.

    Main Results:

    • Cefonicid exhibited stability against Type I beta-lactamase (Enterobacter cloacae) and enzymes from Bacteroides fragilis.
    • Compared to cefamandole, cefonicid showed 6-7 times greater stability against Type IIIA and B enzymes (Escherichia coli).
    • Cefonicid was a non-competitive inhibitor of cephalothin hydrolysis by Type I beta-lactamase, with a Ki of 0.8 x 10(-6)M.

    Conclusions:

    • Cefonicid possesses favorable stability profiles against several clinically relevant beta-lactamases.
    • Its enhanced stability relative to cefamandole suggests potential advantages in treating infections caused by certain resistant bacteria.
    • The non-competitive inhibitory activity of cefonicid against Type I beta-lactamase warrants further investigation.

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