کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9902331 | 1545800 | 2005 | 14 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
An interaction between Sâ¢tag and Sâ¢protein derived from human ribonuclease 1 allows site-specific conjugation of an enzyme to an antibody for targeted drug delivery
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کلمات کلیدی
FBSTFRPNPMesGIMDMRNaseADEPTIscove's modified Dulbecco's medium - Medculus Dulbecco اصلاح شده Iscove استAlkaline phosphatase - آلکالین فسفاتاز یا فسفاتاز قلیاییSDS-PAGE - الکتروفورز ژل پلی آکریل آمیدstandard deviation - انحراف معیارAntibody-directed enzyme prodrug therapy - درمان آنتی بادی آنزیمی پیشگیرانهribonuclease - ریبونوکلئازfetal bovine serum - سرم جنین گاوsite-specific conjugation - هماهنگی خاص سایتPurine nucleoside phosphorylase - پورین نوکلئوزید فسفوریلاtransferrin receptor - گیرنده انتقالین
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
بیوتکنولوژی یا زیستفناوری
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
We have previously demonstrated that an antibody-avidin fusion protein could be used to deliver biotinylated enzymes to tumor cells for antibody-directed enzyme prodrug therapy. However, the presence of the chicken protein avidin suggests that immunogenicity may be a problem. To address this concern, we developed a new delivery system consisting of human proteins. The amino-terminal 15-amino-acid peptide derived from human ribonuclease 1 (human S
- tag) can bind with high affinity to human S
- protein (residues 21-124 of the same ribonuclease). We constructed an antibody-S
- protein fusion protein in which S
- protein was genetically linked to an anti-rat transferrin receptor IgG3 at the carboxyl terminus of the heavy chain. We also constructed an enzyme-S
- tag fusion protein in which S
- tag was genetically linked to the carboxyl terminus of Escherichia coli purine nucleoside phosphorylase (PNP). When these two fusion proteins were mixed, S
- tag and S
- protein interacted specifically and produced homogeneous antibody/PNP complexes that retained the ability to bind antigen. Furthermore, in the presence of the prodrug 2-fluoro-2â²-deoxyadenosine in vitro, the complex efficiently killed rat myeloma cells overexpressing the transferrin receptor. These results suggest that human ribonuclease-based site-specific conjugation can be used in vivo for targeted chemotherapy of cancer.
- tag) can bind with high affinity to human S
- protein (residues 21-124 of the same ribonuclease). We constructed an antibody-S
- protein fusion protein in which S
- protein was genetically linked to an anti-rat transferrin receptor IgG3 at the carboxyl terminus of the heavy chain. We also constructed an enzyme-S
- tag fusion protein in which S
- tag was genetically linked to the carboxyl terminus of Escherichia coli purine nucleoside phosphorylase (PNP). When these two fusion proteins were mixed, S
- tag and S
- protein interacted specifically and produced homogeneous antibody/PNP complexes that retained the ability to bind antigen. Furthermore, in the presence of the prodrug 2-fluoro-2â²-deoxyadenosine in vitro, the complex efficiently killed rat myeloma cells overexpressing the transferrin receptor. These results suggest that human ribonuclease-based site-specific conjugation can be used in vivo for targeted chemotherapy of cancer.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Immunological Methods - Volume 299, Issues 1â2, April 2005, Pages 63-76
Journal: Journal of Immunological Methods - Volume 299, Issues 1â2, April 2005, Pages 63-76
نویسندگان
Tsuneaki Asai, Letitia A. Wims, Sherie L. Morrison,