Abstract
A new approach is applied to the design and study of the antibacterial activity of novel Temporin-Pta peptides. Using Temporin-Pta as a template, together with spiral structure domain breaking and amino acid residue substitution principles, antibacterial peptides are reformed to create new antibacterial peptides. The broth dilution analysis method was used to determine the bacteriostatic effect of the new Temporin-Pta structures, and the hemolytic effect and protease stability of the new peptides were studied. Results showed that the modified antibacterial peptide HX-12A has higher inhibitory effects of active protease stability on E. coli and other bacteria and the hemolytic ability is below 5%, thus achieving successful new Temporin-Pta transformations. It is also shown that the corresponding bacteriostatic effects of these antibacterial peptides are closely related to the differences in structure and composition. This method can improve the biological activity of the antibacterial peptide and drug resistance that is normally difficult to achieve. The present study provides a good theoretical basis for further research on antimicrobial peptide structures and functions.
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