ArticleMolecules (Basel, Switzerland)2016
Photoactivatable Caged Prodrugs of VEGFR-2 Kinase Inhibitors.
Article in Molecules (Basel, Switzerland), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Femtosecond to Microsecond Observation of Photochemical Pathways in Nitroaromatic Phototriggers Using Transient Absorption Spectroscopy.The journal of physical chemistry. A · 2024Article
- Towards medical imaging of drug photoactivation: Development of light responsive magnetic resonance imaging and chemical exchange saturation transfer contrast agents.Smart molecules : open access · 2024Article
- Identification of Maleimide-Fused Carbazoles as Novel Noncanonical Bone Morphogenetic Protein Synergizers.ACS pharmacology & translational science · 2023Article
- Review
- A Photocleavable Contrast Agent for Light-Responsive MRI.Pharmaceuticals (Basel, Switzerland) · 2020Article
- Design, Synthesis, and In Vitro Evaluation of the Photoactivatable Prodrug of the PARP Inhibitor Talazoparib.Molecules (Basel, Switzerland) · 2020Article
- Photoinduced Conversion of Antimelanoma Agent Dabrafenib to a Novel Fluorescent BRAFACS medicinal chemistry letters · 2016Article
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Authors and funding
5 authors.
Funding
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Abstract
In this study, we report on the design, synthesis, photokinetic properties and in vitro evaluation of photoactivatable caged prodrugs for the receptor tyrosine kinase VEGFR-2. Highly potent VEGFR-2 inhibitors 1 and 3 were caged by introduction of a photoremovable protecting group (PPG) to yield the caged prodrugs 4 and 5. As expected, enzymatic and cellular proliferation assays showed dramatically diminished efficacy of caged prodrugs in vitro. Upon ultraviolet (UV) irradiation of the prodrugs original inhibitory activity was completely restored and even distinctly reinforced, as was the case for the prodrug 4. The presented results are a further evidence for caging technique being an interesting approach in the protein kinase field. It could enable spatial and temporal control for the inhibition of VEGFR-2. The described photoactivatable prodrugs might be highly useful as biological probes for studying the VEGFR-2 signal transduction.
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Registered trials
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