The Anti-Microbial Peptide (Lin-SB056-1)<sub>2</sub>-K Reduces Pro-Inflammatory Cytokine Release through Interaction with <i>Pseudomonas aeruginosa</i> Lipopolysaccharide
The ability of many anti-microbial peptides (AMPs) to modulate the host immune response has highlighted their possible therapeutic use to reduce uncontrolled inflammation during chronic infections. In the present study, we examined the anti-inflammatory potential of the semi-synthetic peptide lin-SB...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-09-01
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| Series: | Antibiotics |
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| Online Access: | https://www.mdpi.com/2079-6382/9/9/585 |
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| author | Lucia Grassi Arianna Pompilio Esingül Kaya Andrea C. Rinaldi Enrico Sanjust Giuseppantonio Maisetta Aurélie Crabbé Giovanni Di Bonaventura Giovanna Batoni Semih Esin |
| author_facet | Lucia Grassi Arianna Pompilio Esingül Kaya Andrea C. Rinaldi Enrico Sanjust Giuseppantonio Maisetta Aurélie Crabbé Giovanni Di Bonaventura Giovanna Batoni Semih Esin |
| author_sort | Lucia Grassi |
| collection | DOAJ |
| description | The ability of many anti-microbial peptides (AMPs) to modulate the host immune response has highlighted their possible therapeutic use to reduce uncontrolled inflammation during chronic infections. In the present study, we examined the anti-inflammatory potential of the semi-synthetic peptide lin-SB056-1 and its dendrimeric derivative (lin-SB056-1)<sub>2</sub>-K, which were previously found to have anti-microbial activity against <i>Pseudomonas aeruginosa</i> in in vivo-like models mimicking the challenging environment of chronically infected lungs (i.e., artificial sputum medium and 3-D lung mucosa model). The dendrimeric derivative exerted a stronger anti-inflammatory activity than its monomeric counterpart towards lung epithelial- and macrophage-cell lines stimulated with <i>P. aeruginosa</i> lipopolysaccharide (LPS), based on a marked decrease (up to 80%) in the LPS-induced production of different pro-inflammatory cytokines (i.e., IL-1β, IL-6 and IL-8). Accordingly, (lin-SB056-1)<sub>2</sub>-K exhibited a stronger LPS-binding affinity than its monomeric counterpart, thereby suggesting a role of peptide/LPS neutralizing interactions in the observed anti-inflammatory effect. Along with the anti-bacterial and anti-biofilm properties, the anti-inflammatory activity of (lin-SB056-1)<sub>2</sub>-K broadens its therapeutic potential in the context of chronic (biofilm-associated) infections. |
| first_indexed | 2024-03-10T16:29:46Z |
| format | Article |
| id | doaj.art-83e0cef3acad4a7e96531fd5491858db |
| institution | Directory Open Access Journal |
| issn | 2079-6382 |
| language | English |
| last_indexed | 2024-03-10T16:29:46Z |
| publishDate | 2020-09-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Antibiotics |
| spelling | doaj.art-83e0cef3acad4a7e96531fd5491858db2023-11-20T12:54:47ZengMDPI AGAntibiotics2079-63822020-09-019958510.3390/antibiotics9090585The Anti-Microbial Peptide (Lin-SB056-1)<sub>2</sub>-K Reduces Pro-Inflammatory Cytokine Release through Interaction with <i>Pseudomonas aeruginosa</i> LipopolysaccharideLucia Grassi0Arianna Pompilio1Esingül Kaya2Andrea C. Rinaldi3Enrico Sanjust4Giuseppantonio Maisetta5Aurélie Crabbé6Giovanni Di Bonaventura7Giovanna Batoni8Semih Esin9Department of Translational Research and New Technologies in Medicine and Surgery, University of Pisa, 56123 Pisa PI, ItalyDepartment of Medical, Oral and Biotechnological Sciences, and Center for Advanced Studies and Technology (CAST), “G. d’Annunzio” University of Chieti-Pescara, 66100 Chieti CH, ItalyDepartment of Translational Research and New Technologies in Medicine and Surgery, University of Pisa, 56123 Pisa PI, ItalyDepartment of Biomedical Sciences, University of Cagliari, 09142 Monserrato CA, ItalyDepartment of Biomedical Sciences, University of Cagliari, 09142 Monserrato CA, ItalyDepartment of Translational Research and New Technologies in Medicine and Surgery, University of Pisa, 56123 Pisa PI, ItalyLaboratory of Pharmaceutical Microbiology, Ghent University, 9000 Gent, BelgiumDepartment of Medical, Oral and Biotechnological Sciences, and Center for Advanced Studies and Technology (CAST), “G. d’Annunzio” University of Chieti-Pescara, 66100 Chieti CH, ItalyDepartment of Translational Research and New Technologies in Medicine and Surgery, University of Pisa, 56123 Pisa PI, ItalyDepartment of Translational Research and New Technologies in Medicine and Surgery, University of Pisa, 56123 Pisa PI, ItalyThe ability of many anti-microbial peptides (AMPs) to modulate the host immune response has highlighted their possible therapeutic use to reduce uncontrolled inflammation during chronic infections. In the present study, we examined the anti-inflammatory potential of the semi-synthetic peptide lin-SB056-1 and its dendrimeric derivative (lin-SB056-1)<sub>2</sub>-K, which were previously found to have anti-microbial activity against <i>Pseudomonas aeruginosa</i> in in vivo-like models mimicking the challenging environment of chronically infected lungs (i.e., artificial sputum medium and 3-D lung mucosa model). The dendrimeric derivative exerted a stronger anti-inflammatory activity than its monomeric counterpart towards lung epithelial- and macrophage-cell lines stimulated with <i>P. aeruginosa</i> lipopolysaccharide (LPS), based on a marked decrease (up to 80%) in the LPS-induced production of different pro-inflammatory cytokines (i.e., IL-1β, IL-6 and IL-8). Accordingly, (lin-SB056-1)<sub>2</sub>-K exhibited a stronger LPS-binding affinity than its monomeric counterpart, thereby suggesting a role of peptide/LPS neutralizing interactions in the observed anti-inflammatory effect. Along with the anti-bacterial and anti-biofilm properties, the anti-inflammatory activity of (lin-SB056-1)<sub>2</sub>-K broadens its therapeutic potential in the context of chronic (biofilm-associated) infections.https://www.mdpi.com/2079-6382/9/9/585anti-microbial peptidedendrimeric peptide<i>Pseudomonas aeruginosa</i>LPSanti-inflammatory activity |
| spellingShingle | Lucia Grassi Arianna Pompilio Esingül Kaya Andrea C. Rinaldi Enrico Sanjust Giuseppantonio Maisetta Aurélie Crabbé Giovanni Di Bonaventura Giovanna Batoni Semih Esin The Anti-Microbial Peptide (Lin-SB056-1)<sub>2</sub>-K Reduces Pro-Inflammatory Cytokine Release through Interaction with <i>Pseudomonas aeruginosa</i> Lipopolysaccharide Antibiotics anti-microbial peptide dendrimeric peptide <i>Pseudomonas aeruginosa</i> LPS anti-inflammatory activity |
| title | The Anti-Microbial Peptide (Lin-SB056-1)<sub>2</sub>-K Reduces Pro-Inflammatory Cytokine Release through Interaction with <i>Pseudomonas aeruginosa</i> Lipopolysaccharide |
| title_full | The Anti-Microbial Peptide (Lin-SB056-1)<sub>2</sub>-K Reduces Pro-Inflammatory Cytokine Release through Interaction with <i>Pseudomonas aeruginosa</i> Lipopolysaccharide |
| title_fullStr | The Anti-Microbial Peptide (Lin-SB056-1)<sub>2</sub>-K Reduces Pro-Inflammatory Cytokine Release through Interaction with <i>Pseudomonas aeruginosa</i> Lipopolysaccharide |
| title_full_unstemmed | The Anti-Microbial Peptide (Lin-SB056-1)<sub>2</sub>-K Reduces Pro-Inflammatory Cytokine Release through Interaction with <i>Pseudomonas aeruginosa</i> Lipopolysaccharide |
| title_short | The Anti-Microbial Peptide (Lin-SB056-1)<sub>2</sub>-K Reduces Pro-Inflammatory Cytokine Release through Interaction with <i>Pseudomonas aeruginosa</i> Lipopolysaccharide |
| title_sort | anti microbial peptide lin sb056 1 sub 2 sub k reduces pro inflammatory cytokine release through interaction with i pseudomonas aeruginosa i lipopolysaccharide |
| topic | anti-microbial peptide dendrimeric peptide <i>Pseudomonas aeruginosa</i> LPS anti-inflammatory activity |
| url | https://www.mdpi.com/2079-6382/9/9/585 |
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