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<p>Fc-fusion peptides, also known as peptibodies, are a promising new category of targeted therapeutics that offer alternatives to monoclonal antibodies (mAbs) for cancer treatment. This study focuses on an Fc-fusion peptide consisting of the Fc region of IgG1 and an epidermal growth factor receptor (EGFR)-targeting peptide, GE11, which was identified using the phage display method and demonstrated high affinity for the receptor. The fusion peptide (FcIgG-GE11) was successfully expressed in <i>Escherichia coli</i> and purified using ion-exchange chromatography. Flow cytometry confirmed its specific binding to EGFR. Like Cetuximab, the FcIgG-GE11 peptibody exhibited effective, dose- and time-dependent growth inhibition of EGFR-overexpressing cancer cell lines. Additionally, the results showed that the FcIgG-GE11 peptibody induced cell death or cycle arrest in certain cancer cell lines, with varying responses depending on the cancer type. The results of In-Cell ELISA when comparing the effects of the FcIgG-GE11 peptibody to Cetuximab on Tyr 1173 phosphorylation were similar. In addition, the relative potency of the FcIgG-GE11 peptibody compared to Cetuximab was assessed using the MTT results by Slope Ratio Analysis. These findings suggest that FcIgG-GE11 peptibody can provide a specific and efficient tool for both targeting and treating cancer cells.</p>

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Targeted cancer treatment using a novel EGFR-specific Fc-fusion peptide based on GE11 peptide

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年2月11日

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  • Malihe Hallaji,
  • Mojgan Allahyari,
  • Ladan Teimoori-Toolabi,
  • Setayesh Yasami-Khiabani,
  • Majid Golkar,
  • Pezhman Fard-Esfahani

摘要

Fc-fusion peptides, also known as peptibodies, are a promising new category of targeted therapeutics that offer alternatives to monoclonal antibodies (mAbs) for cancer treatment. This study focuses on an Fc-fusion peptide consisting of the Fc region of IgG1 and an epidermal growth factor receptor (EGFR)-targeting peptide, GE11, which was identified using the phage display method and demonstrated high affinity for the receptor. The fusion peptide (FcIgG-GE11) was successfully expressed in Escherichia coli and purified using ion-exchange chromatography. Flow cytometry confirmed its specific binding to EGFR. Like Cetuximab, the FcIgG-GE11 peptibody exhibited effective, dose- and time-dependent growth inhibition of EGFR-overexpressing cancer cell lines. Additionally, the results showed that the FcIgG-GE11 peptibody induced cell death or cycle arrest in certain cancer cell lines, with varying responses depending on the cancer type. The results of In-Cell ELISA when comparing the effects of the FcIgG-GE11 peptibody to Cetuximab on Tyr 1173 phosphorylation were similar. In addition, the relative potency of the FcIgG-GE11 peptibody compared to Cetuximab was assessed using the MTT results by Slope Ratio Analysis. These findings suggest that FcIgG-GE11 peptibody can provide a specific and efficient tool for both targeting and treating cancer cells.