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Antimicrobial peptides (AMPs) have started to garner more interest as novel antimicrobial agents. The scorpion venom peptide ctry2459 was modified to CT-K3K7 by lysine substitutions at the 3rd and 7th positions to increase the cationic properties. We discovered that the modified peptides CT-K3K7 had improved antibacterial activity, higher thermal stability, as well as lower hemolytic activity. It can kill S. aureus and P. aeruginosa rapidly, and reduce the production of biofilm and live bacterial residues in biofilm in vitro. CT-K3K7 has also been demonstrated to decrease bacterial counts, abscess area, and inflammatory cell infiltration in the mouse subcutaneous abscess models that were duplicated by S. aureus and P. aeruginosa. CT-K3K7 has difficulty in inducing S. aureus and P. aeruginosa to develop drug resistance, which may be related to the bactericidal properties. CT-K3K7 increases cationic properties by lysine substitutions can increase the electrostatic force between the peptides and the bacterial surface, which can lead to an increase in bacterial membrane permeability and DNA binding. In conclusion, the modified peptide CT-K3K7 enhances the antimicrobial activity and can be a novel antimicrobial agent candidate for the treatment of infections by S. aureus and P. aeruginosa.

Antimicrobial peptides (AMPs) have gained interest as a new type of antimicrobial agent. Scorpion venom peptide ctry2459 were modified to CT-K3K7 by lysine substitutions at position 3rd and 7th. We found that the modified peptides CT-K3K7 with improved antibacterial activity, higher thermal stability and lower hemolytic activity. It can rapidly kill S. aureus and P. aeruginosa, reduce the production of biofilm and live bacteria residues in biofilm in vitro. CT-K3K7 has also been demonstrated that could decrease the bacterial counts in the subcutaneous abscess region, abscess area, and inflammatory cell infiltration in mouse subcutaneous abscess models duplicated by S. aureus and P. aeruginosa. CT-K3K7 is difficult to induce S. aureus and P. aeruginosa to develop drugs resistance, which may be related to the bactericidal way that the increase of cationic properties by lysine substitutions can increase the electrostatic force between the peptides and the bacterial surface that lead to the increase of bacterial membrane permeability and DNA binding. In conclusion, the modified peptide CT-K3K7 enhanced antimicrobial activity and can be as a new antimicrobial agent candidate for the treatment of infections by S. aureus and P. aeruginosa.