Open AccessIdentification of antiviral mimetic peptides with interferon α‐2b‐like activity from a random peptide library using a novel functional biopanning method 1
Author(s) -
ZHANG Qi,
BAI Gang,
CHEN Jiaqi,
TIAN Wang,
CAO Yu,
PAN Pengwei,
WANG Chao
Publication year - 2008
Publication title -
acta pharmacologica sinica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.514
H-Index - 90
eISSN - 1745-7254
pISSN - 1671-4083
DOI - 10.1111/j.1745-7254.2008.00755.x
Subject(s) - biopanning , phage display , peptide library , biology , peptide , alpha interferon , microbiology and biotechnology , vesicular stomatitis virus , amino acid , peptide sequence , interferon , virology , virus , biochemistry , gene
Aim: To screen for interferon (IFN) α‐2b mimetic peptides with antiviral activity. Methods: Selecting IFN receptor‐binding peptides from a phage‐display heptapeptide library using a novel functional biopanning method. This method was developed to identify peptides with activity against vesicular stomatitis virus (VSV) inducing cytopathic effects on WISH cells. Results: Sixteen positive clones were obtained after 3 rounds of functional selection. Ten clones were picked from these positive clones according to the results of phage ELISA and were sequenced. The amino acid sequences homologous to IFNα‐2b were defined by residues AB loop 31–37, BC loop 68–74, C helix 93–99, CD loop 106–112, D helix 115–121, DE loop 132–138, and E helix 143–161. Two of the peptides, designated clones T3 and T9, aligned with the IFNAR2‐binding domains (AB loop and E helix), were synthesized and designated as IR‐7 and KP‐7, respectively. Both KP‐7 and IR‐7 were found to compete with GFP/IFNα‐2b for receptor binding and mimicked the antiviral activity of IFNα‐2b cooperatively. Conclusion: Two IFNα‐2b mimetic peptides with antiviral activity were derived from a phage‐display heptapeptide library using a novel functional selection method.