| Autor: |
Varponi I; Department of Biology, University of Padova, Via U. Bassi 58/B, 35131 Padova, Italy., Ferro S; Department of Biomedical Sciences, University of Padova, Via U. Bassi 58/B, 35131 Padova, Italy., Menilli L; Department of Biology, University of Padova, Via U. Bassi 58/B, 35131 Padova, Italy., Grapputo A; Department of Biology, University of Padova, Via U. Bassi 58/B, 35131 Padova, Italy.; National Biodiversity Future Centre, Piazza Marina 61, 90133 Palermo, Italy., Moret F; Department of Biology, University of Padova, Via U. Bassi 58/B, 35131 Padova, Italy., Mastrotto F; Department of Pharmaceutical and Pharmacological Sciences, University of Padova, Via F. Marzolo 5, 35131 Padova, Italy., Marin O; Department of Biomedical Sciences, University of Padova, Via U. Bassi 58/B, 35131 Padova, Italy., Sandrelli F; Department of Biology, University of Padova, Via U. Bassi 58/B, 35131 Padova, Italy. |
| Abstrakt: |
Pseudomonas aeruginosa is an opportunistic Gram-negative bacterium responsible for severe nosocomial infections and is considered a critical pulmonary pathogen for both immunocompromised and cystic fibrosis patients. Planktonic cells of P. aeruginosa possess intrinsic and acquired resistances, inactivating several classes of conventional antibiotics. Additionally, this bacterium can grow, forming biofilms, and complex structures, further hampering the action of multiple antibiotics. Here, we report the biological properties of D-Q53 CecB, an all-D enantiomer of the silkworm natural peptide Q53 CecB. Compared to the L-variant, D-Q53 CecB was resistant to in vitro degradation by humans and P. aeruginosa elastases and showed an enhanced bactericidal activity against P. aeruginosa planktonic bacteria. D-Q53 CecB was thermostable and maintained its antimicrobial activity at high salt concentrations and in the presence of divalent cations or fetal-bovine serum, although at reduced levels. Against different types of human cells, D-Q53 CecB showed cytotoxic phenomena at concentrations several folds higher compared to those active against P. aeruginosa. When L- and D-Q53 CecB were compared for their antibiofilm properties, both peptides were active in inhibiting biofilm formation. However, the D-enantiomer was extremely effective in inducing biofilm degradation, suggesting this peptide as a favorable candidate in an anti- Pseudomonas therapy. |
