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核心技术专利：CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2025

使用基于GE11肽的新型表皮生长因子受体（EGFR）特异性Fc融合肽进行靶向癌症治疗。

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

作者信息

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

机构信息

Department of Biochemistry, Pasteur Institute of Iran, Tehran, Iran.

Recombinant Protein Production Department, Research and Production Complex, Pasteur Institute of Iran, Karaj, Iran.

出版信息

Sci Rep. 2025 Feb 11;15(1):5107. doi: 10.1038/s41598-025-89143-5.

DOI:10.1038/s41598-025-89143-5
PMID:39934226
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11814073/
Abstract

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.

摘要

Fc融合肽，也称为肽抗体，是一类很有前景的新型靶向治疗药物，为癌症治疗提供了单克隆抗体（mAb）的替代方案。本研究聚焦于一种由IgG1的Fc区域和表皮生长因子受体（EGFR）靶向肽GE11组成的Fc融合肽，该肽通过噬菌体展示方法鉴定，对该受体具有高亲和力。融合肽（FcIgG-GE11）在大肠杆菌中成功表达，并使用离子交换色谱法进行纯化。流式细胞术证实了其与EGFR的特异性结合。与西妥昔单抗一样，FcIgG-GE11肽抗体对EGFR过表达的癌细胞系表现出有效的、剂量和时间依赖性的生长抑制作用。此外，结果表明，FcIgG-GE11肽抗体在某些癌细胞系中诱导细胞死亡或细胞周期停滞，不同癌症类型的反应各不相同。比较FcIgG-GE11肽抗体和西妥昔单抗对Tyr 1173磷酸化影响的细胞内ELISA结果相似。此外，使用MTT结果通过斜率比分析评估了FcIgG-GE11肽抗体与西妥昔单抗相比的相对效价。这些发现表明，FcIgG-GE11肽抗体可以为靶向和治疗癌细胞提供一种特异性且有效的工具。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c13f/11814073/6a6a33bac8c4/41598_2025_89143_Fig12_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c13f/11814073/2a640ec82d2e/41598_2025_89143_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c13f/11814073/3ec5fc3ec270/41598_2025_89143_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c13f/11814073/23d861b7435f/41598_2025_89143_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c13f/11814073/021f1c8508a0/41598_2025_89143_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c13f/11814073/33901cfe7172/41598_2025_89143_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c13f/11814073/e92aab81a511/41598_2025_89143_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c13f/11814073/57f252e055a3/41598_2025_89143_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c13f/11814073/64ef508c45c0/41598_2025_89143_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c13f/11814073/a3a16f2130a7/41598_2025_89143_Fig9_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c13f/11814073/e6abdd3c0e32/41598_2025_89143_Fig10_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c13f/11814073/55d357be9e57/41598_2025_89143_Fig11_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c13f/11814073/6a6a33bac8c4/41598_2025_89143_Fig12_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c13f/11814073/2a640ec82d2e/41598_2025_89143_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c13f/11814073/3ec5fc3ec270/41598_2025_89143_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c13f/11814073/23d861b7435f/41598_2025_89143_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c13f/11814073/021f1c8508a0/41598_2025_89143_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c13f/11814073/33901cfe7172/41598_2025_89143_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c13f/11814073/e92aab81a511/41598_2025_89143_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c13f/11814073/57f252e055a3/41598_2025_89143_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c13f/11814073/64ef508c45c0/41598_2025_89143_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c13f/11814073/a3a16f2130a7/41598_2025_89143_Fig9_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c13f/11814073/e6abdd3c0e32/41598_2025_89143_Fig10_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c13f/11814073/55d357be9e57/41598_2025_89143_Fig11_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c13f/11814073/6a6a33bac8c4/41598_2025_89143_Fig12_HTML.jpg

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