The search for new alternative molecules to antibiotics has led to natural antimicrobial peptides (PAP), which are found in all living organisms such as bacteria, fungi, plants and animals, they form their first line of defense of innate immunity. The main mechanism of antimicrobial action of the peptide is the destruction of the cell membrane. This action is mediated by hydrophobic amino acids and a cationic charge, which facilitate the binding of the peptide to the cell membrane of microorganisms (consisting of anionic lipids — phosphatidylglycerol and cardiolipin). After attachment to the cell membrane, the peptide forms pores that ensure the outflow of anions through the membrane, which leads to depolarization of the membrane and, thus, kills bacteria. In contrast, peptides have a low affinity for the mammalian cell membrane, which is rich in electrically neutral phospholipids (phosphatidylcholine and sphingomyelin). Non-membrane mechanisms of antibacterial action have also been described for some peptides, including penetration into a bacterial cell after binding to cell surface receptors. Inside the cell, peptides inhibit critical cell functions such as DNA replication, protein synthesis and folding, protease activity, cell division, and cellular metabolism. Natural antimicrobial peptides may have some undesirable characteristics, such as instability due to degradation by host proteases, hemolytic activity, and toxicity to humans. The creation of synthetic peptides from amino acid sequences of a natural antimicrobial peptide has two goals: 1) Extract antimicrobial activity; 2) exclude the peptide from this particular sequence: toxicity and low resistance to proteolysis. An innovative short cationic peptidomimetic, CAMP-1, has been synthesized in the SCFB laboratory, requiring further study. The purpose of the study: to study the antimicrobial activity and toxic properties of peptidomimetic CAMP-1.