Novel β‑Hairpin Antimicrobial Peptide Containing the β‑Turn Sequence of -NG- and the Tryptophan Zippers Facilitate Self-Assembly into Nanofibers, Exhibiting Excellent Antimicrobial Performance

Antimicrobial peptides (AMPs) have emerged as promising
agents
to combat the antibiotic resistance crisis due to their rapid bactericidal
activity and low propensity for drug resistance. However, AMPs face
challenges in terms of balancing enhanced antimicrobial efficacy with
increased toxicity during modification processes. In this study, de
novo d-type β-hairpin AMPs are designed. The conformational
transformation of self-assembling peptide W-4 in the
environment of the bacterial membrane and the erythrocyte membrane
affected its antibacterial activity and hemolytic activity and finally
showed a high antibacterial effect and low toxicity. Furthermore, W-4 displays remarkable stability, minimal occurrence of drug
resistance, and synergistic effects when combined with antibiotics.
The in vivo studies confirm its high safety and potent
wound-healing properties at the sites infected by bacteria. This study
substantiates that nanostructured AMPs possess enhanced biocompatibility.
These advances reveal the superiority of self-assembled AMPs and contribute
to the development of nanoantibacterial materials.