Scholarlink

<p>The use of intact antibodies, such as trastuzumab, in radioimmunotherapy often causes off-target radiation due to prolonged circulation and increased non-specific binding. This study developed a refined pepsin-based method to generate F(abʹ)₂ fragments of trastuzumab and evaluated the radiochemical stability of [<sup>131</sup>I]I-F(abʹ)<sub>2</sub>-trastuzumab. A pepsin-to-antibody ratio of 1:20 yielded highly pure (&gt; 95%) F(abʹ)₂ fragments, confirming effective enzymatic cleavage. The radiolabeled fragment maintained radiochemical purity above 95% under all storage conditions over 24h, demonstrating high stability. These findings establish a reliable strategy for producing radioiodinated antibody fragments with improved pharmacokinetic properties for targeted HER2-positive breast cancer therapy.</p> Graphical abstract <p></p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Synthesis and stability evaluation of pepsin-fragmented [131I]I-F(abʹ)₂-trastuzumab for HER2-overexpressing breast cancer therapy

  • 期刊论文

  • 发表日期：

    2026年3月25日

查看全文
  • Intan Ghaisani Nadyaputri,
  • Ligwina Dita Pertiwi,
  • Ilma Darojatin,
  • Wening Lestari,
  • Astari Dwiranti,
  • Ratna Dini Haryuni

摘要

The use of intact antibodies, such as trastuzumab, in radioimmunotherapy often causes off-target radiation due to prolonged circulation and increased non-specific binding. This study developed a refined pepsin-based method to generate F(abʹ)₂ fragments of trastuzumab and evaluated the radiochemical stability of [131I]I-F(abʹ)2-trastuzumab. A pepsin-to-antibody ratio of 1:20 yielded highly pure (> 95%) F(abʹ)₂ fragments, confirming effective enzymatic cleavage. The radiolabeled fragment maintained radiochemical purity above 95% under all storage conditions over 24h, demonstrating high stability. These findings establish a reliable strategy for producing radioiodinated antibody fragments with improved pharmacokinetic properties for targeted HER2-positive breast cancer therapy.

Graphical abstract