Evidence map›Paper›PMID 42484769›Full record

ArticleMedical oncology (Northwood, London, England)2026

Design and evaluation of an EpCAM-specific peptide-diphtheria toxin fusion (DT-SNFYMPL) for targeted epithelial cancer treatment.

Sara Rafia, Pegah Tabanmehr, Mahdi Habibi-Anbouhi, Zohre Eftekhari, Alireza Erfani, Fatemeh Kazemi-Lomedasht

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Article in Medical oncology (Northwood, London, England), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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5 · Who and what money

Authors and funding

6 authors.

Sara RafiaVenom and Biotherapeutics Molecules Laboratory, Biotechnology Department, Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran.
Pegah TabanmehrVenom and Biotherapeutics Molecules Laboratory, Biotechnology Department, Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran.
Mahdi Habibi-AnbouhiNational Cell Bank of Iran, Pasteur Institute of Iran, Tehran, Iran.
Zohre EftekhariVenom and Biotherapeutics Molecules Laboratory, Biotechnology Department, Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran.
Alireza ErfaniNational Cell Bank of Iran, Pasteur Institute of Iran, Tehran, Iran.
Fatemeh Kazemi-LomedashtVenom and Biotherapeutics Molecules Laboratory, Biotechnology Department, Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran. fatemeh1044@yahoo.com.ORCID http://orcid.org/0000-0002-5832-1822

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Epithelial cell adhesion molecule (EpCAM, CD326) is a transmembrane glycoprotein that plays important roles in both normal epithelial tissues and epithelial malignancies. Its frequent overexpression in several cancers, including pancreatic, colorectal, and prostate carcinomas, has made it an attractive therapeutic target. In this study, we designed and evaluated a novel EpCAM-binding diphtheria toxin fusion construct, DT-SNFYMPL, in which the EpCAM-binding peptide SNFYMPL was fused to a truncated diphtheria toxin. The recombinant construct was cloned, expressed in Escherichia coli BL21 cells, purified, refolded, and characterized in vitro. Structural modeling and validation predicted a stable three-dimensional structure for the designed protein. Binding analysis demonstrated interaction of DT-SNFYMPL with recombinant EpCAM in an ELISA-based assay. Cytotoxicity studies revealed dose- and time-dependent inhibition of MCF-7 and TC-1 cell proliferation, whereas no significant effect was observed in HUVEC cells under the conditions tested. DT-SNFYMPL also reduced the migration of cancer cells in Transwell assays; however, this effect is likely attributable, at least in part, to toxin-mediated cytotoxicity rather than direct inhibition of migratory pathways. Although the findings demonstrate biological activity of the DT-SNFYMPL construct and support its potential as an EpCAM-binding therapeutic candidate, the present study does not establish EpCAM-dependent internalization, receptor-mediated cytotoxicity, or therapeutic selectivity. Further mechanistic and preclinical studies are required to evaluate its mode of action, safety, and therapeutic potential in EpCAM-expressing malignancies.

Indexed as

Antineoplastic AgentsDiphtheria ToxinEpithelial Cell Adhesion MoleculeNeoplasms, Glandular and EpithelialRecombinant Fusion ProteinsCell Line, TumorCell MovementCell ProliferationHumansMCF-7 CellsAntineoplastic AgentsDiphtheria ToxinEPCAM protein, humanEpithelial Cell Adhesion MoleculeRecombinant Fusion ProteinsDiphtheria toxinEpCAMTargeted drug deliveryTumor-specific peptide

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.