Selected article for: "amino acid and structure analysis"

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_45
    Snippet: Six putative peptides from the venomous cDNA library of the scorpion E. validus were identified as candidate antimicrobial peptides by bioinformatics analysis of their sequences as well as evaluation of their amphipathy and positively charged α-helix structures, which are the classical structure features of antimicrobial peptides. Precursor structure analysis of the six scorpion-derived peptides is shown in Figure 1 . The details of open-readin.....
    Document: Six putative peptides from the venomous cDNA library of the scorpion E. validus were identified as candidate antimicrobial peptides by bioinformatics analysis of their sequences as well as evaluation of their amphipathy and positively charged α-helix structures, which are the classical structure features of antimicrobial peptides. Precursor structure analysis of the six scorpion-derived peptides is shown in Figure 1 . The details of open-reading frames and amino acid sequences are shown. The candidate peptides were screened for viral inactivation against HSV-1 by plaque reduction assay (PRA) in Vero cells.

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