Histidine-rich Modification of a Scorpion-derived Peptide Improves Bioavailability and Inhibitory Activity against HSV-1

Zeng, Zhengyang; Zhang, Runhong; Hong, Wei; Cheng, Yuting; Wang, Huijuan; Lang, Yange; Ji, Zhenglin; Wu, Yingliang; Li, Wenxin; Xie, Youli; Cao, Zhijian

Vero cell monolayers plated in six-well plates were infected with HSV-1 aliquots to yield approximately 60 plaques per well. The peptides were dissolved in pure water over a series of concentrations. The scorpion-derived antiviral peptides were screened at 10 μg/mL. To measure the antiviral activity of Eval418, the peptide was added at a series of concentrations after a 2-fold dilution (10, 5, 2.5, 1.25 and 0.625 µg/mL). The peptides derived from Eval418 were added at a series of concentrations after a 2-fold dilution (5, 2.5, 1.25, 0.625 and 0.3125 µg/mL) to measure their antiviral activities. In all time of addition experiments as well as confocal microscopic spotting and flow cytometry analyses, the peptides were used at a concentration of 10 µg/mL. Isometric sterile water was used as a negative control in all experiments. Antiviral assays were performed by five different ways of treatments.