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Current Pharmaceutical Design


ISSN (Print): 1381-6128
ISSN (Online): 1873-4286

Research Article

Development of a Novel Human scFv Against EGFR L2 Domain by Phage Display Technology

Author(s): Leila Rahbarnia, Safar Farajnia*, Hossein Babaei, Jafar Majidi, Kamal Veisi, Shiva Ahdi Khosroshahi and Asghar Tanomand

Volume 23, Issue 13, 2017

Page: [2009 - 2014] Pages: 6

DOI: 10.2174/1381612822666160928112208

Price: $65


Epidermal growth factor receptor (EGFR) as a transmembrane tyrosine kinase receptor frequently overexpresses in tumors with epithelial origin. The L2 domain from extracellular part of EGFR is involved in ligand binding and the blockage of this domain prevents activation of related signaling pathways. This study was aimed to develop a novel human scFv against EGFR L2 domain as a promising target for cancer therapy. The L2 recombinant protein was purified and used for panning a human scFv phage library (Tomlinson I). In this study, a novel screening strategy was applied to select clones with high binding and enrichment of rare specific phage clones of the L2 protein. After five biopanning rounds several specific clones were isolated which among them one phage clone with high binding was purified for further analysis. The specific interaction of selected clone against target antigen was confirmed by ELISA and western blotting. Immunofluorescence staining showed that purified scFv binds to A431 cells surface, displaying EGFR surface receptor. In the present study, we isolated for the first time a novel human scFv against EGFR L2 domain. This study can be the groundwork for developing more effective diagnostic and therapeutic agents against EGFR overexpressing cancers using this novel human anti-L2 ScFv.

Keywords: Human single chain antibody, cancer, EGFR L2 domain, phage display.

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