Author: Zeng, Zhengyang; Zhang, Runhong; Hong, Wei; Cheng, Yuting; Wang, Huijuan; Lang, Yange; Ji, Zhenglin; Wu, Yingliang; Li, Wenxin; Xie, Youli; Cao, Zhijian
Title: Histidine-rich Modification of a Scorpion-derived Peptide Improves Bioavailability and Inhibitory Activity against HSV-1 Document date: 2018_1_1
ID: zilqyfjl_68
Snippet: In our study, Eval418 was designed and modified into four histidine-rich derivative peptides by introducing 2-5 histidine residues. All four derivative peptides exhibited the same α-helix structures as the wild-type peptide Eval418, indicating that the addition of histidine residues did not affect the peptide structure but enhanced its helicity. In addition, all four derivative peptides showed improved virucidal effects. The IC50 values of Eval4.....
Document: In our study, Eval418 was designed and modified into four histidine-rich derivative peptides by introducing 2-5 histidine residues. All four derivative peptides exhibited the same α-helix structures as the wild-type peptide Eval418, indicating that the addition of histidine residues did not affect the peptide structure but enhanced its helicity. In addition, all four derivative peptides showed improved virucidal effects. The IC50 values of Eval418-FH2, Eval418-FH3, Eval418-FH4 and Eval418-FH5 were 1.50, 1.01, 0.87 and 0.86 μg/mL, respectively. The blocking activities of the four derivative peptides against HSV-1 viral attachment were also improved. Their IC50 values were enhanced from 3.70 μg/mL to 1.43, 0.86, 0.63 and 0.67 μg/mL, respectively. The abilities of the derivative peptides to inhibit viral entry were also significantly improved compared with that of Eval418. In addition, the derivative peptides showed additional inhibition of established HSV-1 infection when added to cells 1 h after infection.
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