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Mass spectrometry enables the discovery of inhibitors of an LPS transport assembly <i>via</i> disruption of protein–protein interactions

Francesco Fiorentino, Dante Rotili, Antonello Mai, Jani Reddy Bolla, Carol V. Robinson

2021Chemical Communications15 citationsDOIOpen Access PDF

Abstract

We developed a native mass spectrometry-based approach to quantify the monomer-dimer equilibrium of the LPS transport protein LptH. We use this method to assess the potency and efficacy of an antimicrobial peptide and small molecule disruptors, obtaining new information on their structure-activity relationships. This approach led to the identification of quinoline-based hit compounds representing the basis for the development of novel LPS transport inhibitors.

Topics & Concepts

ChemistryMass spectrometryProtein–protein interactionBiophysicsCombinatorial chemistryComputational biologyBiochemistryChromatographyBiologyMass Spectrometry Techniques and ApplicationsEnzyme Structure and FunctionRNA and protein synthesis mechanisms
Mass spectrometry enables the discovery of inhibitors of an LPS transport assembly <i>via</i> disruption of protein–protein interactions | Litcius