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- Title
Preparation, Characterization, and Radiolabeling of Anti-HER2 scFv With Technetium Tricarbonyl and Stability Studies.
- Authors
Bozorgchami, Negar; Ahmadzadeh, Maryam; Hatamabadi, Dara; Yazdani, Abdolreza; Shahhosseini, Soraya; Mohit, Elham
- Abstract
Breast cancer is the most common diagnosed cancer, and the second cause of cancer death among women, worldwide. HER2 overexpression occurred in approximately 15% to 20% of breast cancers. Invasive biopsy method has been used for detection of HER2 overexpression. HER2-targeted imaging via an appropriate radionuclide is a promising method for sensitive and accurate identification of HER2+ primary and metastatic lesions. 99mTc-anti-HER2 scFv can specifically target malignancies and be used for diagnosis of the cancer type and metastasis as well as treatment of breast cancer. We radiolabeled anti-HER2 scFv that was expressed in Escherichia coli and purified through Ni-NTA resin under native condition with 99mTc-tricarbonyl formed from boranocarbonate. HER2-based ELISA, BCA, TLC, and HPLC were used in this study. In the current study, anti-HER2 scFv was lyophilized before radiolabeling. It was found that freeze-drying did not change the binding activity of anti-HER2 scFv to HER2. Results demonstrated direct anti-HER2 scFv radiolabeling by 99mTc-tricarbonyl to hexahistidine sequence (His-tag) without any changes in biological activity and radiochemical purity of around 98%. Stability analysis revealed that 99mTc-anti-HER2 scFv is stable for at least 24 h in PBS buffer, normal saline, human plasma proteins, and histidine solution.
- Subjects
RADIOLABELING; RADIOCHEMICAL purification; TECHNETIUM; BLOOD proteins; FREEZE-drying; EPIDERMAL growth factor receptors; PROGESTERONE receptors
- Publication
Journal of Labelled Compounds & Radiopharmaceuticals, 2024, Vol 67, Issue 5, p168
- ISSN
0362-4803
- Publication type
Article
- DOI
10.1002/jlcr.4090