Engineered Peptides Harboring Cation Motifs Against Multidrug-Resistant Bacteria.
Lu ShangChan ChenRui SunJuan GuoJing LiuMi WangLifang ZhangChenzhong FeiFeiqun XueYingchun LiuFeng GuPublished in: ACS applied materials & interfaces (2024)
Multidrug-resistant (MDR) pathogens pose a serious threat to the health and life of humans, necessitating the development of new antimicrobial agents. Herein, we develop and characterize a panel of nine amino acid peptides with a cation end motif. Bioactivity analysis revealed that the short peptide containing "RWWWR" as a central motif harboring mirror structure "KXR" unit displayed not only high activity against MDR planktonic bacteria but also a clearance rate of 92.33% ± 0.58% against mature biofilm. Mechanically, the target peptide (KLR) killed pathogens by excessively accumulating reactive oxygen species and physically disrupting membranes, thereby enhancing its robustness for controlling drug resistance. In the animal model of sepsis infection by MDR bacteria, the peptide KLR exhibited strong therapeutic effects. Collectively, this study provided the dominant structure of short antimicrobial peptides (AMPs) to replenish our arsenals for combating bacterial infections and illustrated what could be harnessed as a new agent for fighting MDR bacteria.
Keyphrases
- multidrug resistant
- gram negative
- drug resistant
- acinetobacter baumannii
- amino acid
- klebsiella pneumoniae
- reactive oxygen species
- staphylococcus aureus
- public health
- healthcare
- ionic liquid
- pseudomonas aeruginosa
- intensive care unit
- mental health
- acute kidney injury
- antimicrobial resistance
- single cell
- risk assessment
- health information
- cystic fibrosis
- biofilm formation
- climate change
- social media