Journal of Drug Delivery Science and Technology, cilt.123, 2026 (SCI-Expanded, Scopus)
The emergence of antibiotic-resistant pathogens has accelerated the search for new antimicrobial strategies. Antimicrobial peptides (AMPs), such as Myxinidin (Myx), offer promising therapeutic potential; however, their clinical application is limited by proteolytic instability and low bioavailability. To address these limitations, recombinant Myx was expressed in Escherichia coli Rosetta (DE3) using the pET28(a) system and purified via Ni-NTA chromatography. The peptide was covalently conjugated to UiO-66-NH2 metal–organic frameworks (MOFs) through EDC/NHS coupling, yielding nanoscale composites characterized by XRD, FT-IR, SEM, and DLS. Importantly, the UiO-66-NH2–Myx conjugate exhibited significantly enhanced antimicrobial activity, with MIC values reduced from 9.18 to 1.71 μM against E. coli and from 6.37 to 1.08 μM against S. aureus , demonstrating strong dose-dependent bactericidal effects. Cytotoxicity assays showed that while bare MOFs induced toxicity, conjugation with Myx improved cell viability and supported fibroblast proliferation. Furthermore, scratch assays demonstrated complete wound closure at 48 h with the conjugate, surpassing Myx. These findings demonstrate that covalent immobilization of Myx onto UiO-66-NH2 provides an effective strategy to enhance antimicrobial efficacy, reduce cytotoxicity, and improve wound-healing performance.