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.
Mass spectrometry enables the discovery of inhibitors of an LPS transport assembly via disruption of protein-protein interactions / Fiorentino, F.; Rotili, D.; Mai, A.; Bolla, J. R.; Robinson, C. V.. - In: CHEMICAL COMMUNICATIONS. - ISSN 1359-7345. - 57:82(2021), pp. 10747-10750. [10.1039/d1cc04186j]
Mass spectrometry enables the discovery of inhibitors of an LPS transport assembly via disruption of protein-protein interactions
Fiorentino F.Primo
;Rotili D.Secondo
;Mai A.
;
2021
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
