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


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.

SUBMITTER: Fiorentino F 

PROVIDER: S-EPMC7614387 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature

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Mass spectrometry enables the discovery of inhibitors of an LPS transport assembly &lt;i&gt;via&lt;/i&gt; disruption of protein-protein interactions.

Fiorentino Francesco F   Rotili Dante D   Mai Antonello A   Bolla Jani R JR   Robinson Carol V CV  

Chemical communications (Cambridge, England) 20211014 82


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. ...[more]

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