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

被引:14
|
作者
Sen, Samya [1 ,2 ]
Samat, Ramkamal [3 ]
Jash, Moumita [1 ]
Ghosh, Satyajit [1 ]
Roy, Rajsekhar [1 ]
Mukherjee, Nabanita [3 ]
Ghosh, Surojit [3 ]
Sarkar, Jayita [4 ]
Ghosh, Surajit [2 ,5 ]
机构
[1] Indian Inst Technol, Dept Biosci & Bioengn, Jodhpur 342030, Rajasthan, India
[2] Indian Inst Technol, IHUB Drishti Fdn, Jodhpur 342030, Rajasthan, India
[3] Indian Inst Technol, Smart Healthcare Dept, Interdisciplinary Res Platform, Jodhpur 342030, Rajasthan, India
[4] Indian Inst Technol, Ctr Res & Dev Sci Instruments, Jodhpur 342030, Rajasthan, India
[5] Indian Inst Technol, Dept Biosci & Bioengn, Smart Healthcare Dept, Interdisciplinary Res Platform, Jodhpur 342030, Rajasthan, India
关键词
INFLAMMATION; MEMBRANE; SKIN; LPS; MACROPHAGES; TRYPTOPHAN; MECHANISM; BIOFILMS; INSIGHTS; REPAIR;
D O I
10.1021/acs.jmedchem.3c01150
中图分类号
R914 [药物化学];
学科分类号
100701 ;
摘要
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.
引用
收藏
页码:11555 / 11572
页数:18
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