Literature DB >> 9383424

Synthesis and beta-lactamase-mediated activation of a cephalosporin-taxol prodrug.

M L Rodrigues1, P Carter, C Wirth, S Mullins, A Lee, B K Blackburn.   

Abstract

BACKGROUND: Enzyme-activatable prodrugs in conjunction with antibody-enzyme fusion proteins may enhance the anti-tumor efficacy of antibodies and reduce the toxic side effects of conventional chemotherapeutics. Cephalosporins have proven to be highly versatile triggers for the enzymatic activation of such prodrugs.
RESULTS: A cephem prodrug of taxol (PROTAX) was synthesized by substituting the C-3' position of cephalothin with 2'-(gamma-aminobutyryl) taxol. Hydrolysis of PROTAX by beta-lactamase rapidly released 2'-(gamma-aminobutyryl) taxol (kcat/K(M) = (1.4 +/- 0.1) x 10(5) s-1 M-1), which yielded taxol following intramolecular displacement. PROTAX is inactive in a microtubule assembly assay in vitro but has similar activity to taxol following prolonged activation with beta-lactamase. PROTAX is approximately 10-fold less toxic than taxol against SK-BR-3 breast tumor cells in vitro but has activity approaching that of taxol following prolonged activation with a fusion protein comprising beta-lactamase fused to a tumor-targeting antibody fragment.
CONCLUSIONS: Tubulin polymerization activity is abolished and cytotoxicity is reduced in the PROTAX prodrug compared to taxol. Activation of PROTAX by beta-lactamase followed by self-immolation restores the activity of PROTAX to that of free taxol.

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Year:  1995        PMID: 9383424     DOI: 10.1016/1074-5521(95)90272-4

Source DB:  PubMed          Journal:  Chem Biol        ISSN: 1074-5521


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