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

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


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نویسندگان: لیلا رهبرنیا , صفر فرج نیا , حسین بابائی , جعفر مجیدی ذوالبین , شیوا عهدی خسروشاهی

کلمات کلیدی: Human single chain antibody, cancer, EGFR L2 domain, Phage display

نشریه: 0 , - , 23 , 2017

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نویسنده ثبت کننده مقاله صفر فرج نیا
مرحله جاری مقاله تایید نهایی
دانشکده/مرکز مربوطه مرکز تحقیقات کاربردی دارویی
کد مقاله 61192
عنوان فارسی مقاله Development of a Novel Human scFv Against EGFR L2 Domain by Phage Display Technology
عنوان لاتین مقاله Development of a Novel Human scFv Against EGFR L2 Domain by Phage Display Technology
ناشر 7
آیا مقاله از طرح تحقیقاتی و یا منتورشیپ استخراج شده است؟ بلی
عنوان نشریه (خارج از لیست فوق) Current pharmacutical design
نوع مقاله Original Article
نحوه ایندکس شدن مقاله ایندکس شده سطح یک – ISI - Web of Science
آدرس لینک مقاله/ همایش در شبکه اینترنت http://www.current-pharmaceutical-design.com/articles/145875/development-of-a-novel-human-scfv-against-egfr-l2-domain-by-phage-d

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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

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نویسنده نفر چندم مقاله
لیلا رهبرنیااول
صفر فرج نیادوم
حسین بابائیسوم
جعفر مجیدی ذوالبینچهارم
شیوا عهدی خسروشاهیششم

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CPD paper.pdf1396/05/212772706دانلود