A fusion protein containing angiopoietin-2 (Ang2) and vascular endothelial growth factor (VEGF) derived peptides covalently attached, via a proprietary diketone linker, to a proprietary humanized catalytic aldolase monoclonal antibody, with potential antiangiogenic and antineoplastic activities. The Ang2/VEGF peptide moieties of Ang2/VEGF-binding peptides-antibody fusion protein CVX-241 bind to Ang2 and VEGF receptors, which may inhibit tumor angiogenesis and tumor cell proliferation. The proprietary humanized catalytic IgG1 monoclonal aldolase antibody contains reactive lysine residues in its binding sites, which react covalently with compounds having a diketone function; the Ang2 and VEGFR peptide moieties are then covalently attached to the diketone linkers via a proprietary spacer. Both VEGF and Ang2 are upregulated in a variety of cancer cell types and play a crucial role in angiogenesis. This agent possesses an enhanced half-life compared to the naked peptides.