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

The inhibitory activities of the Eval418 derivative peptides when added to cells during the HSV-1 attachment or entry steps were also evaluated ( Figure 6e, 6f) . The IC50 values of Eval418-FH2, Eval418-FH3, Eval418-FH4 and Eval418-FH5 during the viral attachment step were 1.43, 0.86, 0.63 and 0.67 μg/mL, respectively, which were also significantly decreased from 3.70 μg/mL of the wild type peptide. The SIs of the derivative peptides were 19.30, 31.20, 43.78 and 159.22, respectively (Table 1 ). The IC50 values of Eval418-FH2, Eval418-FH3, Eval418-FH4 and Eval418-FH5 during the viral entry step were 8.63, 4.23, 4.37 and 2.89 µg/mL, respectively. The inhibitory activities of the derivative peptides during the viral entry step were significantly improved when compared with that of the wild type peptide Eval418 (IC50 = 31.71 µg/mL) ( Table 1) .