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Enhanced binding to and killing of hepatocellular carcinoma cells in vitro by melittin when linked with a novel targeting peptide screened from phage display
Author(s) -
Zhao Honglei,
Feng Xin,
Han Wenyu,
Diao Yuwen,
Han Dong,
Tian Xiaofeng,
Gao Yu,
Liu Shanshan,
Zhu Seng,
Yao Cuimei,
Gu Jingmin,
Sun Changjiang,
Lei Liancheng
Publication year - 2013
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.2542
Subject(s) - melittin , biopanning , peptide , microbiology and biotechnology , in vitro , phage display , peptide library , chemistry , hepatocellular carcinoma , cell sorting , biology , cancer research , flow cytometry , biochemistry , peptide sequence , gene
A random phage 12‐mer peptide library and a whole‐cell subtractive biopanning protocol against HepG2 cells were used to select a novel peptide‐specific binding to hepatocellular carcinoma cells. As a result, peptide SLSLITMLKISR (AM‐2) was screened as a novel homing peptide to hepatocellular carcinoma cells, tested by immunofluorescence and immunochemistry assays. Subsequently, peptide AM‐2 was linked to melittin by A(EAAAK)2A, and the antitumor effect of this ligation product was detected by MTT assay, fluorescence‐activated cell sorting, and scanning electron microscopy methods. Results of cell growth inhibition tests confirmed that the affinity of melittin was increased after being incorporated into AM‐2, and AM‐2‐melittin specifically targeted and killed HepG2 cells in vitro . Thus, AM‐2 is a valuable ligand for tumor targeting, which leads to increased binding and killing effect of hepatocellular carcinoma cells in vitro when ligated to melittin, and AM‐2‐melittin has a clinical potential application as target agents for the treatment of human hepatocellular carcinoma. Copyright © 2013 European Peptide Society and John Wiley & Sons, Ltd.

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