Characterization And Bioactivity Evaluation Of Actinomycin X2/silk Fibroin Protein Based

As a substitute for traditional antibiotics,antimicrobial peptides have attracted much attention,and their versatility is often used in the study of drug molecular activity.However,the application of antimicrobial peptides is limited by their biological toxicity and self-instability,while the stability of cyclic peptide chains is naturally better than that of directly linked peptides.Therefore,the application of cyclic peptides and the combination with materials can highlight the advantages of drugs and eliminate the disadvantages of drug molecules.Actinomycin belongs to a family of chromogenic lactone peptides that differs in their peptide portions of the molecule.An antimicrobial peptide,actinomycin X2(Ac.X2),was produced through the fermentation of a Streptomyces cyaneofuscatus strain.Immobilization of Ac.X2 onto a prepared silk fibroin(SF)film was done through a carbodiimide reaction.The physical properties of immobilized Ac.X2(antimicrobial films,AMFs)were analyzed by ATR-FTIR,SEM,AFM,and WCA.Our findings from an in vitro study showed that AMFs had a more broad-spectrum antibacterial activity against both S.aureus and E.coli compared with free Ac.X2,which showed no apparent strong effect against E.coli.These AMFs showed a suitable degradation rate,good hemocompatibility,and low cytotoxicity in the biocompatibility assay.The results of in vivo bacterially infected wound healing experiments indicated that wound inflammation was prevented by AMFs,which promoted wound repair and improved the wound microenvironment.This study revealed that Ac.X2 transformation is a potential candidate for skin wound healing.