ArticleBioconjugate chemistry2011
Development of a pterin-based fluorescent probe for screening dihydropteroate synthase.
Article in Bioconjugate chemistry, 2011. 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.
- A virtual screening and molecular dynamics approach in search of novel antibiotic chemotypes.PloS one · 2026Article
- Development of Pyrimido Pyridazine Analogs through Increased Whole Cell Target Engagement of the Dihydropteroate Synthase Pterin Binding Site in Gram-Negative Bacteria.ACS infectious diseases · 2025Article
- Synthesis, Redox and Spectroscopic Properties of Pterin of Molybdenum Cofactors.Molecules (Basel, Switzerland) · 2022Review
- Pterin-sulfa conjugates as dihydropteroate synthase inhibitors and antibacterial agents.Bioorganic & medicinal chemistry letters · 2016Article
- Synthesis, spectroscopic properties, and biological applications of eight novel chlorinated fluorescent proteins-labeling probes.Journal of fluorescence · 2014Article
- Structure-based design of novel pyrimido[4,5-c]pyridazine derivatives as dihydropteroate synthase inhibitors with increased affinity.ChemMedChem · 2012Article
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
Dihydropteroate synthase (DHPS) is the classical target of the sulfonamide class of antimicrobial agents, whose use has been limited by widespread resistance and pharmacological side effects. We have initiated a structure-based drug design approach for the development of novel DHPS inhibitors that bind to the highly conserved and structured pterin subsite rather than to the adjacent p-aminobenzoic acid binding pocket that is targeted by the sulfonamide class of antibiotics. To facilitate these studies, a robust pterin site-specific fluorescence polarization (FP) assay has been developed and is discussed herein. These studies include the design, synthesis, and characterization of two fluorescent probes, and the development and validation of a rapid DHPS FP assay. This assay has excellent DMSO tolerance and is highly reproducible as evidenced by a high Z' factor. This assay offers significant advantages over traditional radiometric or phosphate release assays against this target, and is suitable for site-specific high-throughput and fragment-based screening studies.
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Registered trials
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