ArticleEnzyme research2011
Fluorescence Polarization Binding Assay for Aspergillus fumigatus Virulence Factor UDP-Galactopyranose Mutase.
Article in Enzyme research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- Study of Lysozyme Activity in Bird Egg Whites by Fluorescence Polarization Assay Using Chitooligosaccharide Tracer.Foods (Basel, Switzerland) · 2025Article
- Application of the Chitooligosaccharides and Fluorescence Polarization Technique for the Assay of Active Lysozyme in Hen Egg White.Biomolecules · 2024Article
- Fluorescence-Polarization-Based Assaying of Lysozyme with Chitooligosaccharide Tracers.Biomolecules · 2024Article
- Small molecules targeting the NEDD8·NAE protein-protein interaction.Chemical science · 2020Article
- UDP-galactopyranose mutases from Leishmania species that cause visceral and cutaneous leishmaniasis.Archives of biochemistry and biophysics · 2013Article
- Targeting UDP-galactopyranose mutases from eukaryotic human pathogens.Current pharmaceutical design · 2013Review
- A fluorescence polarization binding assay to identify inhibitors of flavin-dependent monooxygenases.Analytical biochemistry · 2012Article
- Chemical mechanism of UDP-galactopyranose mutase from Trypanosoma cruzi: a potential drug target against Chagas' disease.PloS one · 2012Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Aspergillus fumigatus is an opportunistic human pathogenic fungus responsible for deadly lung infections in immunocompromised individuals. Galactofuranose (Galf) residues are essential components of the cell wall and play an important role in A. fumigatus virulence. The flavoenzyme UDP-galactopyranose mutase (UGM) catalyzes the isomerization of UDP-galactopyranose to UDP-galactofuranose, the biosynthetic precursor of Galf. Thus, inhibitors of UGM that block the biosynthesis of Galf can lead to novel chemotherapeutics for treating A. fumigatus-related diseases. Here, we describe the synthesis of fluorescently labeled UDP analogs and the development of a fluorescence polarization (FP) binding assay for A. fumigatus UGM (AfUGM). High-affinity binding to AfUGM was only obtained with the chromophore TAMRA, linked to UDP by either 2 or 6 carbons with K(d) values of 2.6 ± 0.2 μM and 3.0 ± 0.7 μM, respectively. These values were ~6 times lower than when UDP was linked to fluorescein. The FP assay was validated against several known ligands and displayed an excellent Z' factor (0.79 ± 0.02) and good tolerance to dimethyl sulfoxide.
Identifiers
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.