Towards mapping electrostatic interactions between Kdo2-lipid A and cationic antimicrobial peptidesviaultraviolet photodissociation mass spectrometry
| Autor: | Lucas D. Akin, Jennifer S. Brodbelt, Allison P. Myers, Vishnu Srinivasa, Lindsay J. Morrison, Jason B. Shear, Christopher M. Crittenden, Mignon D. Fitzpatrick, Jake Rosenberg, Elisa T. Novelli |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
chemistry.chemical_classification Stereochemistry Photodissociation Cationic polymerization Peptide 010402 general chemistry Mass spectrometry 01 natural sciences Biochemistry Melittin 0104 chemical sciences Analytical Chemistry 03 medical and health sciences chemistry.chemical_compound 030104 developmental biology chemistry Fragmentation (mass spectrometry) Covalent bond Electrochemistry Environmental Chemistry Saccharolipid Spectroscopy |
| Zdroj: | The Analyst. 143:3607-3618 |
| ISSN: | 1364-5528 0003-2654 |
| Popis: | 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 patterns of the apo-peptides. UVPD of the KLA·peptide complexes results in both apo- and holo-sequence ions of the peptides, the latter in which the KLA remains bound to the truncated peptide fragment despite cleavage of a covalent bond of the peptide backbone. Mapping both the N- and C-terminal holo-product ions gives insight into the peptide motifs (specifically an electropositive KRKR segment and a proline residue) that are responsible for mediating the electrostatic interactions between the cationic peptides and saccharolipid. |
| Databáze: | OpenAIRE |
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