Preparation, Characterization, and Radiolabeling of Anti‐HER2 scFv With Technetium Tricarbonyl and Stability Studies

Author:

Bozorgchami Negar12,Ahmadzadeh Maryam23,Hatamabadi Dara1,Yazdani Abdolreza1,Shahhosseini Soraya14ORCID,Mohit Elham2ORCID

Affiliation:

1. Department of Pharmaceutical Chemistry and Radiopharmacy, School of Pharmacy Shahid Beheshti University of Medical Sciences Tehran Iran

2. Department of Pharmaceutical Biotechnology, School of Pharmacy Shahid Beheshti University of Medical Sciences Tehran Iran

3. Food and Drug Laboratory Research Center, Food and Drug Administration The Ministry of Health and Medical Education Tehran Iran

4. Protein Technology Research Centre Shahid Beheshti University of Medical Sciences Tehran Iran

Abstract

ABSTRACTBreast 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.

Funder

Shahid Beheshti University of Medical Sciences

Publisher

Wiley

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