Potential Broad-Spectrum Antimicrobial, Wound Healing, and Disinfectant Cationic Peptide Crafted from Snake Venom

Antimicrobialcationic peptides are intriguing and propitious antibioticsfor the future, even against multidrug-resistant superbugs. Venomsserve as a source of cutting-edge therapeutics and innovative, unexploredmedicines. In this study, a novel cationic peptide library consistingof seven sequences was designed and synthesized from the snake venomcathelicidin, batroxicidin (BatxC), with the inclusion of the FLPIImotif at the N-terminus. SP1V3_1 demonstrated exceptional antibacterialeffectiveness against Escherichia coli, methicillin-resistant Staphylococcus aureus (MRSA), Pseudomonas aeruginosa, and Klebsiella pneumoniae and destroyed the bacteriaby depolarizing, rupturing, and permeabilizing their membranes, asevident from fluorescence assays, atomic force microscopy, and scanningelectron microscopy. SP1V3_1 was observed to modulate the immune responsein LPS-elicited U937 cells and exhibited good antibiofilm activityagainst MRSA and K. pneumoniae. Thepeptide promoted wound healing and disinfection in the murine model.The study demonstrated that SP1V3_1 is an exciting peptide lead andmay be explored further for the development of better therapeuticpeptides.

Automated summary

This study designed and synthesized a novel cationic peptide library consisting of seven sequences from the snake venom cathelicidin, batroxicidin (BatxC), with the inclusion of the FLPII motif at the N-terminus. One of the peptides, SP1V3_1, demonstrated exceptional antibacterial effectiveness against Escherichia coli, methicillin-resistant Staphylococcus aureus (MRSA), Pseudomonas aeruginosa, and Klebsiella pneumoniae by depolarizing, rupturing, and permeabilizing their membranes. SP1V3_1 also showed immune response modulation, antibiofilm activity, and promoted wound healing and disinfection in a murine model.