Fragmentation of Human Neutrophil α-Defensin 4 to Combat Multidrug Resistant Bacteria
Research output: Contribution to journal › Journal article › Research › peer-review
Documents
- Fragmentation of Human Neutrophil α-Defensin 4 to Combat Multidrug Resistant Bacteria
Final published version, 2.89 MB, PDF document
The occurrence and spread of multidrug-resistant bacteria is a prominent health concern. To curb this urgent threat, new innovative strategies pursuing novel antimicrobial agents are of the utmost importance. Here, we unleashed the antimicrobial activity of human neutrophil peptide-4 (HNP-4) by tryptic digestion. We identified a single 11 amino acid long fragment (HNP-41–11) with remarkable antimicrobial potential, exceeding that of the full length peptide on both mass and molar levels. Importantly, HNP-41–11 was equally bactericidal against multidrug-resistant and non-resistant strains; a potency that was further enhanced by N- and C-terminus modifications (acetylation and amidation, respectively). These observations, combined with negligible cytotoxicity not exceeding that of the full length peptide, presents proteolytic digestion of innate host-defense-peptides as a novel strategy to overcome the current health crisis related to antibiotic-resistant bacteria.
Original language | English |
---|---|
Article number | 1147 |
Journal | Frontiers in Microbiology |
Volume | 11 |
Number of pages | 10 |
ISSN | 1664-302X |
DOIs | |
Publication status | Published - 2020 |
- HNP-4, host defense peptides, multidrug resistance, proteolytic digestion, α-defensins
Research areas
Number of downloads are based on statistics from Google Scholar and www.ku.dk
ID: 245616036