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Gelatinases play an important role in tumor growth and metastasis, and overexpressionof these molecules is strongly correlated with poor prognosis in a variety ofmalignant tumors. Lidamycin is an enediyne antitumor antibiotic with potent cytotoxicity.We previously reported that a tandem scFv format (dFv-LDP-AE) showed enhancedbinding ability with gelatinases compared with the scFv-lidamycin conjugate (Fv-LDP-AE).In this study, the antitumor activities of dFv-LDP-AE on hepatocellular carcinoma(HCC) were evaluated in vitro and in vivo. By SDS-PAGE analysis, it was foundthat partial fusion protein dFv-LDP existed as dimer; the results of ELISA andimmunofluorescence demonstrated that the fusion protein dFv-LDP could efficientlybind to hepatoma cells in vitro. The apparent arrest of cell cycle at G2/M phaseand induction of apoptosis at nanomole levels indicated that the dFv-LDP-AE wasvery potent against HCC. In in vivo experiments, dFv-LDP-AE shown enhanced cytotoxiceffects compared to those of LDM. Administration at mouse tolerable dosage level,the inhibition rate of tumor growth was 89.5% of dFv-LDP-AE vs. 73.6% of LDM ontransplantable H22 in mice (P&lt;0.05) and, 87.3% of dFv-LDP-AE vs. 63.4% of LDMon hepatoma Bel-7402 in athymic mice (P&lt;0.01). Small animal optical imagingshowed that the FITC-labeled dFv-LDP preferentially localized in the tumor sitein less than 30 min, which demonstrated remarkable tumor-targeting properties.Taken together with the above findings, the enediyne-energized fusion proteindFv-LDP-AE showed potential application as a new agent for therapeutic appicationsin HCC.

Antitumor activities of dFv-LDP-AE: An enediyne-energized fusion protein targeting tumor-associated antigen gelatinases