ArticleChembiochem : a European journal of chemical biology2019
Synthesis and in Vitro Characterization of Trehalose-Based Inhibitors of Mycobacterial Trehalose 6-Phosphate Phosphatases.
Article in Chembiochem : a European journal of chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- AbCro, a novel transcription factor, promotes biofilm formation and virulence in Acinetobacter baumannii.BMC microbiology · 2026Article
- Structures of trehalose-6-phosphate synthase, Tps1, from the fungal pathogenProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Ferrocenium complex aidedRSC advances · 2021Article
- Dismantling the bacterial glycocalyx: Chemical tools to probe, perturb, and image bacterial glycans.Bioorganic & medicinal chemistry · 2021Review
- Trehalose and bacterial virulence.Virulence · 2020Review
- Structural basis of trehalose recycling by the ABC transporter LpqY-SugABC.Science advances · 2020Article
- A suicide inhibitor of nematode trehalose-6-phosphate phosphatases.Scientific reports · 2019Article
- Promising Recent Strategies with Potential Clinical Translational Value to Combat Antibacterial Resistant Surge.Medicines (Basel, Switzerland) · 2019Review
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Authors and funding
5 authors at 2 institutions in 2 countries.
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Abstract
α,α'-Trehalose plays roles in the synthesis of several cell wall components involved in pathogenic mycobacteria virulence. Its absence in mammalian biochemistry makes trehalose-related biochemical processes potential targets for chemotherapy. The trehalose 6-phosphate synthase (TPS)/trehalose 6-phosphate phosphatase (TPP) pathway, also known as the OtsA/OtsB2 pathway, is the major pathway involved in the production of trehalose in Mycobacterium tuberculosis (Mtb). In addition, TPP is essential for Mtb survival. We describe the synthesis of α,α'-trehalose derivatives in the forms of the 6-phosphonic acid 4 (TMP), the 6-methylenephosphonic acid 5 (TEP), and the 6-N-phosphonamide 6 (TNP). These non-hydrolyzable substrate analogues of TPP were examined as inhibitors of Mtb, Mycobacterium lentiflavum (Mlt), and Mycobacterium triplex (Mtx) TPP. In all cases the compounds were most effective in inhibiting Mtx TPP, with TMP [IC
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