Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

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 information Original publication

DOI

10.1039/d1cc04186j

Type

Journal article

Publication Date

2021-10-14T00:00:00+00:00

Volume

57

Pages

10747 - 10750

Total pages

3

Keywords

Anti-Infective Agents, Crystallization, High-Throughput Screening Assays, Humans, Lipopolysaccharide Receptors, Mass Spectrometry, Oxazines, Peptides, Protein Binding, Protein Multimerization, Quinolines, Small Molecule Libraries, Structure-Activity Relationship