"Peptides corresponding to the substrate sequences L/VP4.1 and non-hydrolysable linker (NHL) were synthesized between a 5-carboxyfluorescein (5-FAM) fluorophore/CPC Quencher (CPQ2) quencher pair (CPC Scientific). Additional lysines were added for increased solubility giving final peptide sequences of CPQ2-IVYELQGP-K(5FAM)-KK-NH2 and CPQ2-GGSGGS-K(5FAM)-KK-NH2 for L/VP4.1 and NHL, respectively. The identity and sequence of the L/VP4.1 and NHL peptides were confirmed by CPC Scientific via LC-MS and determined to be 96.7% and 95.1% pure, respectively."
Abstract
The oncolytic picornavirus Seneca Valley Virus (SVV-001) demonstrates anti-tumor activity in models of small cell lung cancer (SCLC), but may ultimately need to be combined with cytotoxic therapies to improve responses observed in patients. Combining SVV-001 virotherapy with a peptide prodrug activated by the viral protease 3Cpro is a novel strategy that may increase the therapeutic potential of SVV-001. Using recombinant SVV-001 3Cpro, we measured cleavage kinetics of predicted SVV-001 3Cpro substrates. An efficient substrate, L/VP4 (kcat/KM = 1932 ± 183 M-1s-1), was further optimized by a P2’ N→P substitution yielding L/VP4.1 (kcat/KM = 17446 ± 2203 M-1s-1). We also determined essential substrate amino acids by sequential N-terminal deletion and substitution of amino acids found in other picornavirus genera. A peptide corresponding to the L/VP4.1 substrate was selectively cleaved by SVV-001 3Cpro in vitro and was stable in human plasma. These data define an optimized peptide substrate for SVV-001 3Cpro, with direct implications for anti-cancer therapeutic development.
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