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  3. Preparation, Characterization, And Radiolabeling Of Anti-her2 Scfv With Technetium Tricarbonyl And Stability Studies.
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  3. Preparation, Characterization, And Radiolabeling Of Anti-her2 Scfv With Technetium Tricarbonyl And Stability Studies.

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

Negar Bozorgchami1,2, Maryam Ahmadzadeh2,3, Dara Hatamabadi1

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

Journal of Labelled Compounds & Radiopharmaceuticals
|March 14, 2024

View abstract on PubMed

Summary
This summary is machine-generated.

This study successfully developed a radiolabeled anti-HER2 single-chain variable fragment (scFv) for breast cancer imaging. The 99mTc-labeled anti-HER2 scFv demonstrated high purity and stability, offering a promising tool for HER2-positive cancer detection.

Keywords:
breast cancerhuman epidermal growth factor receptor 2 (HER2)radiolabelingsingle‐chain variable fragment (scFv)technetium‐99m tricarbonyl

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Area of Science:

  • Oncology
  • Radiochemistry
  • Biotechnology

Background:

  • Breast cancer is a leading cause of cancer death globally, with HER2 overexpression occurring in 15-20% of cases.
  • Current HER2 detection relies on invasive biopsies; HER2-targeted radionuclide imaging offers a less invasive, sensitive alternative.
  • Anti-HER2 single-chain variable fragments (scFv) show potential for specific targeting of HER2-positive malignancies.

Purpose of the Study:

  • To develop and characterize a technetium-99m (99mTc)-labeled anti-HER2 scFv for potential use in breast cancer diagnosis and treatment.
  • To evaluate the effect of lyophilization on the binding activity of anti-HER2 scFv.
  • To assess the radiolabeling efficiency, purity, and stability of the 99mTc-labeled anti-HER2 scFv.

Main Methods:

  • Anti-HER2 scFv was expressed in E. coli, purified, and lyophilized.
  • Radiolabeling was performed using 99mTc-tricarbonyl directly onto the hexahistidine (His-tag) sequence of the scFv.
  • Assays including ELISA, BCA, TLC, and HPLC were used for characterization and purity assessment. Stability was tested in various solutions.

    • Main Results:

    • Lyophilization did not affect the HER2-binding activity of the anti-HER2 scFv.
    • Direct radiolabeling with 99mTc-tricarbonyl achieved high radiochemical purity of approximately 98% without compromising biological activity.
    • The resulting 99mTc-anti-HER2 scFv remained stable for at least 24 hours in various physiological buffers and solutions.

    Conclusions:

    • Direct radiolabeling of lyophilized anti-HER2 scFv with 99mTc-tricarbonyl is an efficient method.
    • The developed 99mTc-anti-HER2 scFv maintains biological activity and exhibits excellent stability, making it a promising candidate for HER2-targeted breast cancer imaging.
    • This approach offers a potential advancement over invasive biopsy methods for detecting HER2-positive breast cancer and its metastases.