Mass spectrometry enables the discovery of inhibitors of an LPS transport assembly via disruption of protein-protein interactions

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 r...

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Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2021-10, Vol.57 (82), p.10747-10750
Main Authors: Fiorentino, Francesco, Rotili, Dante, Mai, Antonello, Bolla, Jani R, Robinson, Carol V
Format: Article
Language:English
Subjects:
Anti-Infective Agents - chemistry
Anti-Infective Agents - pharmacology
Antiinfectives and antibacterials
Crystallization
Dimers
High-Throughput Screening Assays
Humans
Inhibitors
Lipopolysaccharide Receptors - chemistry
Mass spectrometry
Mass Spectrometry - methods
Oxazines - chemistry
Peptides - chemistry
Peptides - pharmacology
Protein Binding
Protein Multimerization
Proteins
Quinoline
Quinolines - chemistry
Quinolines - pharmacology
Scientific imaging
Small Molecule Libraries - chemistry
Small Molecule Libraries - pharmacology
Spectroscopy
Structure-Activity Relationship
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Summary: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.
ISSN:1359-7345
1364-548X
DOI:10.1039/d1cc04186j