ArticleInternational journal of oncology2016
Feasibility of imaging of epidermal growth factor receptor expression with ZEGFR:2377 affibody molecule labeled with 99mTc using a peptide-based cysteine-containing chelator.
Article in International journal of oncology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- DNA-drug conjugates enable logic-gated drug delivery amplified by hybridization chain reactions.Nature biotechnology · 2026Article
- Radioligand-Antibody Conjugates: Integrating Antibody Engineering, Chelator Chemistry, and Radioligands for Precision Theranosis.Molecular diagnosis & therapy · 2026Review
- Affibody-Derived Drug Conjugates Targeting The Epidermal Growth Factor Receptor Are Potent And Specific Cytotoxic Agents.ACS pharmacology & translational science · 2025Article
- Method for Mapping the Membrane Protein Nanoenvironments Using DNA Nanostructures (NanoDeep).Methods in molecular biology (Clifton, N.J.) · 2025Article
- Comparison of approaches for increasing affinity of affibody molecules for imaging of B7-H3: dimerization and affinity maturation.EJNMMI radiopharmacy and chemistry · 2024Article
- Novel Bifunctional Affibody Molecules with Specific Binding to Both EBV LMP1 and LMP2 for Targeted Therapy of Nasopharyngeal Carcinoma.International journal of molecular sciences · 2023Article
- EBV LMP1-C terminal binding affibody molecule downregulates MEK/ERK/p90RSK pathway and inhibits the proliferation of nasopharyngeal carcinoma cells in mouse tumor xenograft models.Frontiers in cellular and infection microbiology · 2022Article
- The Use of a Non-Conventional Long-Lived Gallium RadioisotopePharmaceutics · 2021Article
- Generation of a novel affibody molecule targeting Chlamydia trachomatis MOMP.Applied microbiology and biotechnology · 2021Article
- A DNA-nanoassembly-based approach to map membrane protein nanoenvironments.Nature nanotechnology · 2021Article
- Feasibility of Imaging EpCAM Expression in Ovarian Cancer Using Radiolabeled DARPin Ec1.International journal of molecular sciences · 2020Article
- Benefit of Later-Time-Point PET Imaging of HER3 Expression Using Optimized Radiocobalt-Labeled Affibody Molecules.International journal of molecular sciences · 2020Article
- Affibody Molecules as Targeting Vectors for PET Imaging.Cancers · 2020Review
- Novel EBV LMP-2-affibody and affitoxin in molecular imaging and targeted therapy of nasopharyngeal carcinoma.PLoS pathogens · 2020Article
- Preclinical Evaluation of [Cells · 2018Article
- Influence of composition of cysteine-containing peptide-based chelators on biodistribution ofAmino acids · 2018Article
- Cyclic versus Noncyclic Chelating Scaffold forMolecular pharmaceutics · 2018Article
- Comparative evaluation of tumor targeting using the anti-HER2 ADAPT scaffold protein labeled at the C-terminus with indium-111 or technetium-99m.Scientific reports · 2017Article
- Preparation and Identification of HER2 Radioactive Ligands and Imaging Study of Breast Cancer-Bearing Nude Mice.Translational oncology · 2017Article
- Affibody molecules as engineered protein drugs.Experimental & molecular medicine · 2017Review
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The epidermal growth factor receptor (EGFR) is overexpressed in a number of malignant tumors and is a molecular target for several specific anticancer antibodies and tyrosine kinase inhibitors. The overexpression of EGFR is a predictive biomarker for response to several therapy regimens. Radionuclide molecular imaging might enable detection of EGFR overexpression by a non-invasive procedure and could be used repeatedly. Affibody molecules are engineered scaffold proteins, which could be selected to have a high affinity and selectivity to predetermined targets. The anti-EGFR ZEGFR:2377 affibody molecule is a potential imaging probe for EGFR detection. The use of the generator-produced radionuclide 99mTc should facilitate clinical translation of an imaging probe due to its low price, availability and favorable dosimetry of the radionuclide. In the present study, we evaluated feasibility of ZEGFR:2377 labeling with 99mTc using a peptide-based cysteine-containing chelator expressed at the C-terminus of ZEGFR:2377. The label was stable in vitro under cysteine challenge. In addition, 99mTc-ZEGFR:2377 was capable of specific binding to EGFR-expressing cells with high affinity (274 pM). Studies in BALB/C nu/nu mice bearing A431 xenografts demonstrated that 99mTc-ZEGFR:2377 accumulates in tumors in an EGFR-specific manner. The tumor uptake values were 3.6±1 and 2.5±0.4% ID/g at 3 and 24 h after injection, respectively. The corresponding tumor-to-blood ratios were 1.8±0.4 and 8±3. The xenografts were clearly visualized at both time-points. This study demonstrated the potential of 99mTc-labeled ZEGFR:2377 for imaging of EGFR in vivo.
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