| Autor: |
Christopher M, Crittenden, Lindsay J, Morrison, Mignon D, Fitzpatrick, Allison P, Myers, Elisa T, Novelli, Jake, Rosenberg, Lucas D, Akin, Vishnu, Srinivasa, Jason B, Shear, Jennifer S, Brodbelt |
| Rok vydání: |
2018 |
| Předmět: |
|
| Zdroj: |
The Analyst. 143(15) |
| ISSN: |
1364-5528 |
| 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. Kdo(2)-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 |
| Externí odkaz: |
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