Fig. 3: Identification of novel peptide-based inhibitors of cathepsin G and elastase.

a Hydrolysis of the synthetic cathepsin G substrate, FLF-sBzl, by a fixed concentration of purified cathepsin G (20 nM), in the presence or absence of the indicated concentrations of the candidate cathepsin G peptide inhibitors. b Hydrolysis of the synthetic elastase substrate, AAPV-AMC, by a fixed concentration of purified elastase (20 nM), in the presence or absence of the indicated concentrations of the candidate cathepsin G peptide inhibitors. c Hydrolysis of the synthetic elastase substrate, AAPV-AMC, by a fixed concentration of purified elastase (20 nM), in the presence or absence of the indicated concentrations of the candidate elastase peptide inhibitors. d Hydrolysis of the synthetic cathepsin G substrate, FLF-sBzl, by a fixed concentration of purified cathepsin G (20 nM), in the presence or absence of the indicated concentrations of peptide inhibitors. Cathepsin G inhibitor I (CG Inhib I) or elastase inhibitor IV (NE Inhib IV) served as controls. Results shown are representative of at least three independent experiments