Towards mapping electrostatic interactions between Kdo₂-lipid A and cationic antimicrobial peptides via ultraviolet photodissociation mass spectrometry.

ABSTRACT: Cationic antimicrobial peptides (CAMPs) have been known to act as multi-modal weapons against Gram-negative bacteria. As a new approach to investigate the nature of the interactions between CAMPs and the surfaces of bacteria, native mass spectrometry and two MS/MS strategies (ultraviolet photodissociation (UVPD) and higher energy collisional activation (HCD)) are used to examine formation and disassembly of saccharolipid·peptide complexes. Kdo2-lipid A (KLA) is used as a model saccharolipid to evaluate complexation with a series of cationic peptides (melittin and three analogs). Collisional activation of the KLA·peptide complexes results in the disruption of electrostatic interactions, resulting in apo-sequence ions with shifts in the distribution of ions compared to the fragmentation patt

SUBMITTER: Crittenden CM 

PROVIDER: S-EPMC6056329 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature