ArticleBioorganic & medicinal chemistry letters2014
Structural characterization of P1'-diversified urea-based inhibitors of glutamate carboxypeptidase II.
Article in Bioorganic & medicinal chemistry letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 17 citations in OpenAlex.
- Interactions of Urea-Based Inhibitors with Prostate-Specific Membrane Antigen for Boron Neutron Capture Therapy.ACS omega · 2021Article
- 2-Aminoadipic Acid-C(O)-Glutamate Based Prostate-Specific Membrane Antigen Ligands for Potential Use as Theranostics.ACS medicinal chemistry letters · 2018Article
- Prostate-specific membrane antigen targeted protein contrast agents for molecular imaging of prostate cancer by MRI.Nanoscale · 2016Article
- The Small Molecule Hyperphyllin Enhances Leaf Formation Rate and Mimics Shoot Meristem Integrity Defects Associated with AMP1 Deficiency.Plant physiology · 2016Article
- Design of composite inhibitors targeting glutamate carboxypeptidase II: the importance of effector functionalities.The FEBS journal · 2016Article
- Enhanced semiempirical QM methods for biomolecular interactions.Computational and structural biotechnology journal · 2015Review
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
Abstract
Urea-based inhibitors of human glutamate carboxypeptidase II (GCPII) have advanced into clinical trials for imaging metastatic prostate cancer. In parallel efforts, agents with increased lipophilicity have been designed and evaluated for targeting GCPII residing within the neuraxis. Here we report the structural and computational characterization of six complexes between GCPII and P1'-diversified urea-based inhibitors that have the C-terminal glutamate replaced by more hydrophobic moieties. The X-ray structures are complemented by quantum mechanics calculations that provide a quantitative insight into the GCPII/inhibitor interactions. These data can be used for the rational design of novel glutamate-free GCPII inhibitors with tailored physicochemical properties.
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Registered trials
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