Cell-to-cell signaling, or quorum sensing (QS), in Gram-negative bacteria is governed by {small|little|tiny|modest|smaller|compact} molecule signals (N-acyl L-homoserine lactones, AHLs) and their cognate intracellular receptors (LuxR-type proteins). The mechanistic underpinnings of QS in these bacteria are severely {limited|restricted} {due to|because of|as a result of|on account of|resulting from|as a consequence of} the challenges of isolating and manipulating most LuxR-type proteins. Quantitative assays to characterize the direct binding of ligands to these receptors are largely non-existent. We report herein a Förster Resonance {Energy|Power} Transfer (FRET) assay that leverages (i) conserved endogenous tryptophans {located|situated|positioned} {in the|within the|inside the} LuxR-type protein ligand-binding {site|website|web site|internet site|web-site|web page} and synthetic fluorophore-AHL conjugates, and (ii) isolation/stabilization {of the|from the|in the|on the|with the|of your} proteins bound to weak agonists. The FRET assay permits {straightforward|simple} measurement of ligand-binding affinities with receptor—either in vitro or in cells—and was shown {to be|to become} compatible with six LuxR-type receptors. These {methods|techniques|strategies|approaches|procedures|solutions} will advance {fundamental|basic} investigations {of the|from the|in the|on the|with the|of your} mechanisms of LuxR-type proteins {and the|and also the|as well as the|along with the|plus the} {development|improvement} of {small|little|tiny|modest|smaller|compact} molecule modulators of QS. Price of 5-Cyclopropyl-1H-imidazole 2′-O-MOE-U structure PMID:36628218
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