Abstract
In recent years, significant progress has been achieved in AMP research, revealing the potential of these compounds as alternatives to traditional antibiotics. Due to the diverse mechanisms of action and a wide range of antibacterial activity, AMP provides new opportunities for preventing and treating multidrug-resistant infections by creating foods with antimicrobial properties, new antimicrobial biologically active additives and medicines. This study aimed to create, characterise and classify a new AMP. The DRAMP proteomic database was used to design the AMP, and the Peptide Ranker was utilised to predict biological activity (http://distilldeep.ucd.ie/PeptideRanker). The peptide was identified with the help of the EROP-Moscow database (http://erop.inbi.ras.ru/index.html), and its physio-chemical properties were studied using the APD, DRAMP and PepCalc databases (http://pepcalc.com). The research resulted in the design of a new AMP consisting of 11 amino acid residues with the following percentages: Val, Ala, Trp, Gly, Pro, Tyr, Glu, His, Lys by 9 % and Arg by 18 %. The total hydrophobic ratio in the peptide, determined by APD, is 27 %; the total net charge is +2.25. Its molecular formula is C64H96N21O15S0, with protein binding potential (Boman index) at 3.44 kcal/mol. The peptide can form an alpha helix. The resulting peptide can be classified as a synthesised cationic hydrophobic alpha-helical antimicrobial polypeptide.
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