期刊
PHARMACEUTICS
卷 12, 期 12, 页码 -出版社
MDPI
DOI: 10.3390/pharmaceutics12121217
关键词
mouse mastitis model; antimicrobial peptide; protein nanoparticle; inclusion body; recombinant protein; Escherichia coli; Staphylococcus aureus; therapeutic protein
资金
- INIA (MINECO, Spain) [RTA201500064-C02-02, RTA2015-00064-C02-01]
- AGAUR [2017 SGR-229]
- Bioengineering, Biomaterials and Nanomedicine Networking Biomedical Research Centre (CIBER-BBN) - Carlos III Health Institute, Spain
- European Regional Development
- Natural Sciences and Engineering Research Council of Canada (NSERC grant) [2020-04811]
Oligomerization of antimicrobial peptides into nanosized supramolecular complexes produced in biological systems (inclusion bodies and self-assembling nanoparticles) seems an appealing alternative to conventional antibiotics. In this work, the antimicrobial peptide, GWH1, was N-terminally fused to two different scaffold proteins, namely, GFP and IFN-gamma for its bacterial production in the form of such recombinant protein complexes. Protein self-assembling as regular soluble protein nanoparticles was achieved in the case of GWH1-GFP, while oligomerization into bacterial inclusion bodies was reached in both constructions. Among all these types of therapeutic proteins, protein nanoparticles of GWH1-GFP showed the highest bactericidal effect in an in vitro assay against Escherichia coli, whereas non-oligomerized GWH1-GFP and GWH1-IFN-gamma only displayed a moderate bactericidal activity. These results indicate that the biological activity of GWH1 is specifically enhanced in the form of regular multi-display configurations. Those in vitro observations were fully validated against a bacterial infection using a mouse mastitis model, in which the GWH1-GFP soluble nanoparticles were able to effectively reduce bacterial loads.
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