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Your search keyword '"Soares Da Costa, Tatiana P"' showing total 3 results
Start Over Author "Soares Da Costa, Tatiana P" Journal bioorganic & medicinal chemistry letters
3 results on '"Soares Da Costa, Tatiana P"'

3. Heterocyclic acyl-phosphate bioisostere-based inhibitors of Staphylococcus aureus biotin protein ligase

Author

Andrew D. Abell, William Tieu, Angie M. Jarrad, Tatiana P. Soares da Costa, John C. Wallace, Ashleigh S. Paparella, Kelly A. Keeling, Steven W. Polyak, Grant W. Booker, Tieu, William, Jarrad, Angie M, Paparella, Ashleigh S, Keeling, Kelly A, Soares Da Costa, Tatiana P, Wallace, John C, Booker, Grant W, Polyak, Steven W, and Abell, Andrew D

Subjects
Models, Molecular, Staphylococcus aureus, drug design, Stereochemistry, Clinical Biochemistry, Binding pocket, Biotin, Pharmaceutical Science, Crystallography, X-Ray, medicine.disease_cause, Biochemistry, antibiotics, Ligases, chemistry.chemical_compound, Bacterial Proteins, Heterocyclic Compounds, inhibitors, Drug Discovery, bioisosteres, medicine, Humans, Enzyme Inhibitors, Molecular Biology, chemistry.chemical_classification, DNA ligase, Molecular Structure, Chemistry, Organic Chemistry, Phosphate, Organophosphates, Enzyme, ligases, Molecular Medicine, Bioisostere
Abstract

Inhibitors of Staphylococcus aureus biotin protein ligase (SaBPL) are generated by replacing the acyl phosphate group of biotinyl-5′-AMP with either a 1,2,3-triazole (see 5/10a/10b) or a 1,2,4-oxadiazole (see 7) bioisostere. Importantly, the inhibitors are inactive against the human BPL. The nature of the 5-substituent in the component benzoxazolone of the optimum 1,2,3-triazole series is critical to activity, where this group binds in the ATP binding pocket of the enzyme. Refereed/Peer-reviewed

Published
2014

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