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Fig. 8 | BMC Molecular and Cell Biology

Fig. 8

From: Regulation of the Fasciola hepatica newly excysted juvenile cathepsin L3 (FhCL3) by its propeptide: a proposed ‘clamp-like’ mechanism of binding and inhibition

Fig. 8

Inhibition profile of the 33-mer synthetic peptide derived from the FhCL3 propeptide. The inhibitory activity of the synthetic peptide at a concentration of 500 nM was tested against the recombinant F. hepatica cathepsin peptidases, FhCL1, FhCL2 and FhCL3, and human cathepsin peptidases, HsCL and HsCK. The percentage of inhibition by the peptide is presented relative to the total activity of each enzyme alone. The broad-spectrum cysteine peptidase inhibitor E-64 was used as a positive inhibitor. The experiments were performed in triplicate and the results are presented as mean ± standard deviation. Statistical analysis was carried out using One-way ANOVA with Dunnett multiple comparison (*** P ≤ 0.001, * P ≤ 0.05, ns, no-significant differences)

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