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Sadaqat M H. A review of the structure and mechanism of action of antimicrobial peptides. KJMS 2024; 9 (17) :25-35
URL: http://kjms.knu.edu.af/article-1-37-en.html

Antimicrobial peptides (AMPs) are naturally occurring molecules produced by bacteria, plants, human cells, and other organisms, typically consisting of fewer than 100 amino acids. These peptides serve as crucial defenders against a variety of pathogens, including bacteria, fungi, and viruses. One notable AMP is nisin, a lantibiotic that binds to lipid II on the surface of gram-positive bacteria. This action disrupts peptidoglycan synthesis and creates pores in the bacterial membrane, ultimately leading to cell death. Polymyxins, cyclic lipopeptides, are employed as a last-resort treatment for antibiotic-resistant gram-negative bacteria. They exert their antimicrobial effects by binding to lipopolysaccharides (LPS) and disrupting the bacterial membrane function. Daptomycin, structurally similar to polymyxins, forms pores in the membranes of gram-positive bacteria, causing potassium leakage and subsequent bacterial death. Additionally, indolicidin, derived from bovine immune cells, exhibits activity against various microorganisms by inhibiting DNA and protein synthesis. Similarly, peptides like magainin and pexiganan possess alpha-helical structures that not only create pores in microbial membranes but also induce DNA fragmentation and apoptosis. Despite their promising antimicrobial properties, the use of AMPs is limited by potential toxicity to human cells and the emergence of resistance. Continued research on these peptides is essential, as their unique mechanisms offer the potential for broader therapeutic applications in combating resistant infections in the future.