ArticleJournal of medicinal chemistry2010
2-aminoimidazole amino acids as inhibitors of the binuclear manganese metalloenzyme human arginase I.
Article in Journal of medicinal chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 67 citations in OpenAlex.
- A colorimetric assay adapted to fragment screening revealing aurones and chalcones as new arginase inhibitors.RSC medicinal chemistry · 2024Article
- Consequences of Disturbing Manganese Homeostasis.International journal of molecular sciences · 2023Review
- Polygenic risk score trend and new variants on chromosome 1 are associated with male gout in genome-wide association study.Arthritis research & therapy · 2022Article
- Arginase as a Potential Biomarker of Disease Progression: A Molecular Imaging Perspective.International journal of molecular sciences · 2020Review
- Targeting Metalloenzymes for Therapeutic Intervention.Chemical reviews · 2019Review
- Arginase Structure and Inhibition: Catalytic Site Plasticity Reveals New Modulation Possibilities.Scientific reports · 2017Article
- Pharmacokinetics and Pharmacodynamics of Promising Arginase Inhibitors.European journal of drug metabolism and pharmacokinetics · 2017Review
- Cinnamide Derivatives as Mammalian Arginase Inhibitors: Synthesis, Biological Evaluation and Molecular Docking.International journal of molecular sciences · 2016Article
- Engineering an effective Mn-binding MRI reporter protein by subcellular targeting.Magnetic resonance in medicine · 2015Article
- Impact of substrate protonation and tautomerization states on interactions with the active site of arginase I.Journal of chemical information and modeling · 2013Article
- Synthesis of a new trifluoromethylketone analogue of l-arginine and contrasting inhibitory activity against human arginase I and histone deacetylase 8.Bioorganic & medicinal chemistry letters · 2011Article
- Competitive metabolism of L-arginine: arginase as a therapeutic target in asthma.Journal of biomedical research · 2011Article
- Binding of α,α-disubstituted amino acids to arginase suggests new avenues for inhibitor design.Journal of medicinal chemistry · 2011Article
- Crystallization of an apo form of human arginase: using all the tools in the toolbox simultaneously.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- The second-shell metal ligands of human arginase affect coordination of the nucleophile and substrate.Biochemistry · 2010Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Arginase, a key metalloenzyme of the urea cycle that converts L-arginine into L-ornithine and urea, is presently considered a pharmaceutical target for the management of diseases associated with aberrant l-arginine homeostasis, such as asthma, cardiovascular diseases, and erectile dysfunction. We now report the design, synthesis, and evaluation of a series of 2-aminoimidazole amino acid inhibitors in which the 2-aminoimidazole moiety serves as a guanidine mimetic. These compounds represent a new class of arginase inhibitors. The most potent inhibitor identified in this study, 2-(S)-amino-5-(2-aminoimidazol-1-yl)pentanoic acid (A1P, 10), binds to human arginase I with K(d) = 2 microM and significantly attenuates airways hyperresponsiveness in a murine model of allergic airways inflammation. These findings suggest that 2-aminoimidazole amino acids represent new leads for the development of arginase inhibitors with promising pharmacological profiles.
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Registered trials
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