Catechol-induced assembly to enhance the performance of antimicrobial peptide fully

As a class of novel antimicrobial agents, antimicrobial peptides (AMPs) are meant to be the next generation antibiotics. Defects in toxicity, stability, and antimicrobial activity hinder the clinical use. The assembly method was designed to solve the defects of AMPs. Herein, an effective strategy for introducing catechol-derivative 3,4-dihydroxy- L -phenylalanine (DOPA) into the well-studied MP196 (RWRWRW-NH 2 ) to alleviate the disadvantages is proposed. Smaller particle size is given by introducing zwitterionic peptide with same design. Catechol-induced peptide assembly results in better antimicrobial activity. And catechol groups could also eliminate free radicals leading to the ability to regulate inflammation. Mechanism study confirmed the membrane disruption behavior and the influence of the ΔpH on the proton motive force (PMF) of bacteria. The catechol-induced assemblies can also effectively resist the influence of enzymes and serum on their antibacterial efficacy. Efficacy of peptide assembly in vivo shows over 92 % reduction in bacteria, mitigation of inflammation, and acceleration of wound healing. This work suggested that vesicles made from catechol-induced assembly AMP and zwitterionic peptides may be a new method to solve the drawbacks of AMP for further usage.