چاپ صفحه |  صفحه نخست سامانه |  چکیده مقاله |  نویسندگان |  دانلود مقاله | دانشگاه علوم پزشکی تبریز |
| نویسنده ثبت کننده مقاله | صفر فرج نیا |
| مرحله جاری مقاله | تایید نهایی |
| دانشکده/مرکز مربوطه | مرکز تحقیقات کاربردی دارویی |
| کد مقاله | 58398 |
| عنوان فارسی مقاله | طراحی، بیان و ارزیابی یک آنتی بادی تک زنجیره ای انسانی شده علیه گیرنده فاکتور رشد اپیدرمی |
| عنوان لاتین مقاله | Design, Expression and evaluation of a novel humanized single chain antibody against epidermal Growth Factor receptor |
| ناشر | 7 |
| آیا مقاله از طرح تحقیقاتی و یا منتورشیپ استخراج شده است؟ | بلی |
| عنوان نشریه (خارج از لیست فوق) | Protein Expression and Purification |
| 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.ncbi.nlm.nih.gov/pubmed/25088934 |
| Various strategies have been attempted for targeting of epidermal growth factor receptor (EGFR), as an essential biomarker in a variety of cancers. Several anti-EGFR antibodies including cetuximab are used in clinics for treatment of EGFR-overexpressing colorectal and head and neck cancers but the efficiency of these antibodies is threatened by their large size and chimeric nature. Humanized single chains antibodies (huscFv) are smaller generation of antibodies with lower immunogenicity may overcome these limitations. This article reports production and evaluation of a novel humanized anti-EGFR scFv. The CDRs of cetuximab heavy and light chains were grafted onto human antibody frameworks as framework donors. To maintain the antigen binding affinity of murine antibody, the murine vernier zone residues were retained in framework regions of huscFv. Additionally, two point mutations in CDR-L1 and CDR-L3 and three point mutations in CDR-H2 and CDR-H3 loops of the humanized scFv (huscFv) were introduced to increase affinity of the huscFv to EGFR. Analysis of results demonstrated that the humanness degree of resultant huscFv was increased as 19%. HuscFv was expressed in BL21 (DE3) and affinity purified via Ni- NTA column. The reactivity of huscFv with EGFR was evaluated by ELISA and dot blot techniques. Analysis by ELISA and dot blot showed that the huscFv was able to recognize and react with EGFR. Toxicity analysis by MTT assay indicated an inhibitory effect on growth of EGFR-overexpressing A431 cells. In conclusion, the huscFv produced in this study revealed decreased immunogenicity while retained growth inhibitory effect on EGFR-overexpressing tumor cells. |
| نویسنده | نفر چندم مقاله |
|---|---|
| صفر فرج نیا | دوم |
| بهمن اکبری | اول |
| نصرت اله ضرغامی | سوم |
| محمد رحمتی | پنجم |
| شیوا عهدی خسروشاهی | ششم |
| لیلا رهبرنیا | هفتم |
| نام فایل | تاریخ درج فایل | اندازه فایل | دانلود |
|---|---|---|---|
| farajnia3.pdf | 1395/05/01 | 1989134 | دانلود |
