Protein-Based Films Functionalized with a Truncated Antimicrobial Peptide Sequence Display Broad Antimicrobial Activity

The increasing bacterial resistance to antibiotics is driving strong demand for new antimicrobial biomaterials. This work describes the fabrication of free-standing films exhibiting properties by combining, in same polypeptide chain, an elastin-like recombinamer comprising 200 repetitions pentamer VPAVG (A200) and 18-amino-acid truncated variant peptide BMAP-28, termed BMAP-18. fusion protein BMAP-18A200 was overexpressed conveniently purified a simplified scalable nonchromatographic process. Free-standing demonstrated be stable without requiring cross-linking agents displayed high activity against skin pathogens including Gram-negative Gram-positive bacteria as well unicellular filamentous fungi. mediated direct contact cells with film surface, resulting compromised structural integrity microbial cells. Furthermore, showed no cytotoxicity on normal human cell lines (skin fibroblasts keratinocytes). All these results highlight potential biotechnological multifunctional polymers drug-free materials prevent treat infections.