Abstract
BmKn2 is an antimicrobial peptide (AMP) characterized from the venom of scorpion Mesobuthus martensii Karsch by our group. In this study, Kn2-7 was derived from BmKn2 to improve the antibacterial activity and decrease hemolytic activity. Kn2-7 showed increased inhibitory activity against both Gram-positive bacteria and Gram-negative bacteria. Moreover, Kn2-7 exhibited higher antibacterial activity against clinical antibiotic-resistant strains such as methicillin-resistant Staphylococcus aureus (MRSA). In addition, the topical use of Kn2-7 effectively protected the skin of mice from infection in an S. aureus mouse skin infection model. Kn2-7 exerted its antibacterial activity via a bactericidal mechanism. Kn2-7 killed S. aureus and E. coli rapidly by binding to the lipoteichoic acid (LTA) in the S. aureus cell wall and the lipopolysaccharides (LPS) in the E. coli cell wall, respectively. Finally, the hemolytic activity of Kn2-7 was significantly decreased, compared to the wild-type peptide BmKn2. Taken together, the Kn2-7 peptide can be developed as a topical therapeutic agent for treating bacterial infections.
Highlights
Drug resistance poses an increasing threat to global public health, and new antibiotic-resistant pathogens have continued to emerge [1,2]
The helical wheels of BmKn2 and its mutants were divided into two parts, and the hydrophobic face and the hydrophilic face were labeled (Figure 1B). These peptides were used to determine the inhibitory activities against the representative Gram-positive bacteria S. aureus AB94004 and the representative Gram-negative bacteria E. coli AB94012
The structure-function relationship of some antimicrobial peptides has been analyzed to unravel the regular pattern of antibacterial activity, hemolytic activity and toxicity [23]
Summary
Drug resistance poses an increasing threat to global public health, and new antibiotic-resistant pathogens have continued to emerge [1,2]. The structures of AMPs generally present highly amphiphilic topologies, in which hydrophilic and hydrophobic side chains are located on opposite faces of the molecule [7,8]. These peptides are potent antimicrobial agents against bacteria, fungi, viruses, and parasites, and several AMPs have been reported to inhibit the growth of MRSA [9,10,11]. Their broad spectrum activity and low potential to induce resistance make AMPs an attractive family of compounds with the potential to be developed as therapeutics agents. Several antimicrobial peptides have been investigated as therapeutic agents [12,13]
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