RT info:eu-repo/semantics/article
T1 Protein-Based Films Functionalized with a Truncated Antimicrobial Peptide Sequence Display Broad Antimicrobial Activity
A1 Da Costa, André
A1 Pereira, A.
A1 Sampaio, Paula
A1 Rodríguez Cabello, José Carlos
A1 Gomes, Andreia C.
A1 Casal, Margarida
A1 Machado, Raúl
K1 Microbiología
K1 Antimicrobial materials
K1 Materiales antimicrobianos
K1 Skin infections
K1 Infecciones de la piel
K1 2414 Microbiología
AB The increasing bacterial resistance to antibiotics is driving strong demand for new antimicrobial biomaterials. This work describes the fabrication of free-standing films exhibiting antimicrobial properties by combining, in the same polypeptide chain, an elastin-like recombinamer comprising 200 repetitions of the pentamer VPAVG (A200) and an 18-amino-acid truncated variant of the antimicrobial peptide BMAP-28, termed BMAP-18. The fusion protein BMAP-18A200 was overexpressed and conveniently purified by a simplified and scalable nonchromatographic process. Free-standing films of BMAP-18A200 demonstrated to be stable without requiring cross-linking agents and displayed high antimicrobial activity against skin pathogens including Gram-negative and Gram-positive bacteria as well as unicellular and filamentous fungi. The antimicrobial activity of the films was mediated by direct contact of cells with the film surface, resulting in compromised structural integrity of microbial cells. Furthermore, the BMAP-18A200 films showed no cytotoxicity on normal human cell lines (skin fibroblasts and keratinocytes). All of these results highlight the potential of these biotechnological multifunctional polymers as new drug-free materials to prevent and treat microbial infections.
PB American Chemical Society
SN 2373-9878
YR 2021
FD 2021
LK https://uvadoc.uva.es/handle/10324/55044
UL https://uvadoc.uva.es/handle/10324/55044
LA eng
NO ACS Biomaterials Science & Engineering, 2021, 7, 2, 451–461
NO Producción Científica
DS UVaDOC
RD 23-dic-2024