期刊
CHEMISTRY & BIOLOGY
卷 22, 期 2, 页码 196-205出版社
CELL PRESS
DOI: 10.1016/j.chembiol.2015.01.002
关键词
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资金
- National Institute of Allergy and Infectious Diseases of the NIH [R21AI098701]
- Canadian Institutes for Health Research by the Fund for Scientific Research - Flanders (FWO-Vlaanderen) [MOP-74493]
- Institute for the Promotion of Innovation through Science and Technology in Flanders (IWT-Vlaanderen, SBO programme)
- Interuniversity Attraction Poles Programme initiated by the Belgian Science Policy Office
- Fundacion la Caixa'' and Fundacion Canada (Spain)
In many infections, bacteria form surface-associated communities known as biofilms that are substantially more resistant to antibiotics than their planktonic counterparts. Based on the design features of active antibiofilm peptides, we made a series of related 12-amino acid L-, D- and retro-inverso derivatives. Specific D-enantiomeric peptides were the most potent at inhibiting biofilm development and eradicating preformed biofilms of seven species of wildtype and multiply antibiotic-resistant Gram-negative pathogens. Moreover, these peptides showed strong synergy with conventional antibiotics, reducing the antibiotic concentrations required for complete biofilm inhibition by up to 64-fold. As shown previously for 1018, these D-amino acid peptides targeted the intracellular stringent response signal (p) ppGpp. The most potent peptides DJK-5 and DJK-6 protected invertebrates from lethal Pseudomonas aeruginosa infections and were considerably more active than a previously described L-amino acid peptide 1018. Thus, the protease-resistant peptides produced here were more effective both in vitro and in vivo.
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