The properties of antimicrobial peptides as substances with high biological activity are considered; they can also be used as functional ingredients and (or) preservative substances in food product composition for preventive and specialized purposes. A new antimicrobial peptide consisting of 20 amino acid residues was developed; during the work, suitable amino acid sequences were selected, physical and chemical characteristics were optimized, and activity against target microorganisms was assessed. The inclusion of positively charged amino acids, such as lysine and arginine, which increase the cationicity of antimicrobial peptides and therefore increase their selectivity towards microbial membranes, is considered. The percentage content of each amino acid is as follows, %: Val – 5, Leu – 25, Cys – 5, Ala – 20, Trp – 5, Gly – 5, Ser –5, His – 5, Lys – 20 and Arg – 5. General hydrophobicity ratio determined by APD is 60%, the charge is + 5.25. The peptide has a molecular weight of 2 206.761 Da, protein binding potential (Bohmann index) of 0.23 kcal/mol. The peptide can form alpha helices and has at least 8 elements on a single hydrophobic surface. According to data obtained from the APD database, the peptide can interact with bacterial membranes and is antimicrobial. The following known antimicrobial peptides are closest in physical and chemical characteristics to the created peptide: AP 00500, AP 03880 and AP 03383. The developed peptide can be classified as a cationic alpha-helical hydrophobic antimicrobial peptide.

Ulitina Elizaveta A., Valieva Sholpan S., Tikhonov Sergey L., Tikhonova Natalya V.

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