Journal
ACS APPLIED MATERIALS & INTERFACES
Volume 12, Issue 40, Pages 44459-44474Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acsami.0c12226
Keywords
antimicrobial peptides; specifically targeted activity; cell-penetrating activity; action mechanism; S. agalactiae
Funding
- National Natural Science Foundation of China [31672434, 31872368, 31902195, 31472104]
- China Agricultural Research System [CARS-35]
- Natural Science Foundation of Heilongjiang Province [TD2019C001]
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The significance of the complex bacterial ecosystem in the human body and the impediment of the mammalian membrane against many antibiotics together emphasize the necessity to develop antimicrobial agents with precise antimicrobial and cell-penetrating activities. A simple and feasible method for generating dual-function antimicrobial peptides inspired by highly hydrophobic peptide pheromone and cationic cell-penetrating peptides is presented. Furthermore, the extension of the peptide candidate library is achieved by modifying the charged domain. The bacteria-selective peptides L1, L2, L10, and L11 kill Streptococcus agalactiae by disrupting the membrane structure, and the targeted mechanism is suggested where the peptides offset the entrapment of S. agalactiae rather than of other bacteria. Moreover, L2 and L10 possess intracellular antibacterial activity and carrier property, which is mainly dependent on endocytosis. Given their suitable biocompatibility, high tolerance, no drug resistance, and effective antimicrobial capacity in a mouse mastitis model, L2 and L10 can be powerful weapons against S. agalactiae pathogen infection.
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