ArticleMolecules (Basel, Switzerland)2021
Effective Tumor Targeting by EphA2-Agonist-Biotin-Streptavidin Conjugates.
Article in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 7 citations in OpenAlex.
- Bio-SS-TS as a Targeted Antitumor Drug Exerts an Anti-Liver Cancer Effect by Enhancing Mitochondria-Dependent Apoptosis.Biological procedures online · 2025Article
- EPHA2 Receptor as a Possible Therapeutic Target in Viral Infections.Current medicinal chemistry · 2024Review
- EPH/Ephrin-Targeting Treatment in Breast Cancer: A New Chapter in Breast Cancer Therapy.International journal of molecular sciences · 2022Review
- Targefrin: A Potent Agent Targeting the Ligand Binding Domain of EphA2.Journal of medicinal chemistry · 2022Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
We recently reported on a potent synthetic agent, 135H11, that selectively targets the receptor tyrosine kinase, EphA2. While 135H11 possesses a relatively high binding affinity for the ligand-binding domain of EphA2 (Kd~130 nM), receptor activation in the cell required the synthesis of dimeric versions of such agent (namely 135H12). This was expected given that the natural ephrin ligands also need to be dimerized or clustered to elicit agonistic activity in cell. In the present report we investigated whether the agonistic activity of 135H11 could be enhanced by biotin conjugation followed by complex formation with streptavidin. Therefore, we measured the agonistic EphA2 activity of 135H11-biotin (147B5) at various agent/streptavidin ratios, side by side with 135H12, and a scrambled version of 147B5 in pancreatic- and breast-cancer cell lines. The (147B5)
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