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7179627 
Journal Article 
Potent effects of amino acid scanned antimicrobial peptide Feleucin-K3 analogs against both multidrug-resistant strains and biofilms of Pseudomonas aeruginosa 
Xie, J; Yang, W; Jiang, X; Li, Yao; Li, J; Yan, Z; Wang, Dan; Guo, X; Zhang, J; Zhang, B; Mou, L; , 
2018 
Yes 
Amino Acids
ISSN: 0939-4451
EISSN: 1438-2199 
SPRINGER WIEN 
WIEN 
1471-1483 
30136030 
WOS:000444729300014 
Pseudomonas aeruginosa is particularly difficult to treat because it possesses a variety of resistance mechanisms and because it often forms biofilms. Antimicrobial peptides represent promising candidates for future templates of antibiotic-resistant bacterial infections due to their unique mechanism of antimicrobial action. In this study, we first found that the antimicrobial peptide Feleucin-K3 has potent antimicrobial activity against not only the standard strain of P. aeruginosa but also against the multidrug-resistant strains isolated from clinics. Then, the structure-activity relationship of the peptide was investigated using alanine and D-amino acid scanning. Among the analogs synthesized, FK-1D showed much more potent antimicrobial activity, superior stability, and very low toxicity, and it was able to permeabilize bacterial membranes. Furthermore, it exhibited significant anti-biofilm activity. More importantly, FK-1D showed excellent antimicrobial activity in vivo, especially against clinical multidrug-resistant bacteria, in contrast to ceftazidime. Our results suggested that FK-1D could be subjected to fixed-point modification in the first and fourth sites to further optimize its medicinal properties and potential as a lead compound for the treatment of infections caused by multidrug-resistant P. aeruginosa and the associated biofilms.