Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
7559796 | Analytical Biochemistry | 2010 | 7 Pages |
Abstract
An alarming number of clinically relevant bacterial pathogens are becoming resistant to many antibiotics, thereby fueling intense research into the discovery of novel therapeutic targets. Phosphopantetheinyl transferases (PPTases) represent a promising target for antibacterial development because these enzymes are crucial for the biosynthesis of a multitude of a pathogen's collection of essential metabolites and virulence factors biosynthesized via polyketide synthase (PKS) and nonribosomal peptide synthetase (NRPS) pathways. Here we describe the development of a fluorescence polarization (FP) assay that is amenable for high-throughput screening to identify PPTase inhibitors. The FP assay was validated against a panel of competitive ligands and displayed an excellent Zâ² score.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Benjamin P. Duckworth, Courtney C. Aldrich,