Amphiphilic lysine conjugated to tobramycin synergizes legacy antibiotics against wild-type and multidrug-resistant Pseudomonas aeruginosa.
Yinfeng LyuRonald DomalaonXuan YangFrank SchweizerPublished in: Biopolymers (2017)
Peptidomimetic modification is a common route of optimization for biologically active peptides. Previous studies in our group have shown that conjugation of amphiphilic tobramycin to other antibacterials enhance their latent outer membrane permeabilizing and efflux blocking activity toward Gram-negative pathogens including Pseudomonas aeruginosa. Herein, we describe the antimicrobial adjuvant properties of amphiphilic lysine ligated to tobramycin. The most potent amphiphilic lysine-tobramycin conjugate 3 potentiated the antibacterial efficacy of 8 clinically used antibiotics against wild type, multidrug- and extensively drug-resistant P. aeruginosa isolates from Canadian hospitals whereas amphiphilic lysine 4 did not. Antibiotics that are synergistic with conjugate 3 included moxifloxacin, ciprofloxacin, erythromycin, chloramphenicol, trimethoprim, novobiocin, linezolid, and fosfomycin. Out of these 8 antibiotics, novobiocin showed highest synergy.
Keyphrases
- multidrug resistant
- gram negative
- drug resistant
- wild type
- acinetobacter baumannii
- pseudomonas aeruginosa
- klebsiella pneumoniae
- cystic fibrosis
- amino acid
- biofilm formation
- cancer therapy
- healthcare
- staphylococcus aureus
- early stage
- photodynamic therapy
- methicillin resistant staphylococcus aureus
- drug delivery
- anti inflammatory