Additional Supporting Information may be found in the online version of this article.

HEP_25665_sm_SuppFig1.tif11189KSupporting Information Figure 1. Mapping the anti-viral activity of hEP. In (A) and (B), HCVcc-luc was first mixed with indicated peptides (20 μg/ml, 2.7 μM) and then incubated with Huh7.5.1 cells for two hours at 37°C to initiate infection. After additional 48 hours incubation, luciferase activity was measured. Results are presented as fold of inhibition relative to infections containing DMSO (n=5, mean ± sd). (C) 20 μg of hEP-2 or hEP-2/ΔCys were resuspended in PBS and kept at room temperature for 30minutes. Peptides were then mixed with 2X SDS-sample buffer without DTT and boiled for 5 minutes. Alternatively, samples were simply left unboiled or mixed with sample buffer containing DTT (2 mM). Peptide samples were then subjected to electrophoresis on a 16% tricine non-reducing gel (Invitrogen). The calculated molecular weight of hEP-2 is 4034.82 Da. (D) and (E) Mass spectrometric analysis of hEP-2 or hEP-2/ΔCys. Notice the dimer peak of hEP-2 in (D).
HEP_25665_sm_SuppFig2.tif131KSupporting Information Figure 2. hEP-2 inhibits HCVcc binding to Huh7.5.1 cells. The effects of hEP-2 (2.7 μM) or scrambled peptide on HCV binding were determined as described in Fig. 5D. Results were calculated as relative RNA copies with numbers obtained from the scrambled peptide treated wells set to 100 (mean of n=3; error bars, s.d.). ** p<0.005.
HEP_25665_sm_SuppInfo.doc50KSupporting Information

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