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

(FAFLAAIPSILSAL) were identified from the E. validus venom gland cDNA library and chemically synthesized. The peptides synthesized in this study were prepared by ChinaPeptides Company, a leading supplier of synthetic peptides in China. Briefly, the peptides were synthesized using solid-phase synthesis and C-terminal amidation in a standardized process. Fmoc-rink resin was used as the synthesis resin by Fmoc strategy. Piperidine was used for deprotecting, and HOBt/HBTU was used for coupling. The finished peptides were cleaved from the resin using trifluoroacetic acid (TFA), precipitated with ether and subjected to purification by reverse-phase HPLC on a C-18 hydrophobic resin (Elite-HPLC) in 0.1% TFA using an acetonitrile gradient. The purity of the final material was verified by reverse-phase HPLC, and the mass of the peptide was determined by mass spectrometry (Voyager-DESTR; Applied Biosystems). All peptides had purities of 95% or greater.