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Structure-Dependent Immune Modulatory Activity of Protegrin-1 Analogs
Protegrins are porcine antimicrobial peptides (AMPs) that belong to the cathelicidin family of host defense peptides. Protegrin-1 (PG-1), the most investigated member of the protegrin family, is an arginine-rich peptide consisting of 18 amino acid residues, its main chain adopting a β-hairpin struct...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4472440/ https://www.ncbi.nlm.nih.gov/pubmed/26097747 http://dx.doi.org/10.3390/antibiotics3040694 |
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author | Zughaier, Susu M. Svoboda, Pavel Pohl, Jan |
author_facet | Zughaier, Susu M. Svoboda, Pavel Pohl, Jan |
author_sort | Zughaier, Susu M. |
collection | PubMed |
description | Protegrins are porcine antimicrobial peptides (AMPs) that belong to the cathelicidin family of host defense peptides. Protegrin-1 (PG-1), the most investigated member of the protegrin family, is an arginine-rich peptide consisting of 18 amino acid residues, its main chain adopting a β-hairpin structure that is linked by two disulfide bridges. We report on the immune modulatory activity of PG-1 and its analogs in neutralizing bacterial endotoxin and capsular polysaccharides, consequently inhibiting inflammatory mediators’ release from macrophages. We demonstrate that the β-hairpin structure motif stabilized with at least one disulfide bridge is a prerequisite for the immune modulatory activity of this type of AMP. |
format | Online Article Text |
id | pubmed-4472440 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-44724402015-06-19 Structure-Dependent Immune Modulatory Activity of Protegrin-1 Analogs Zughaier, Susu M. Svoboda, Pavel Pohl, Jan Antibiotics (Basel) Article Protegrins are porcine antimicrobial peptides (AMPs) that belong to the cathelicidin family of host defense peptides. Protegrin-1 (PG-1), the most investigated member of the protegrin family, is an arginine-rich peptide consisting of 18 amino acid residues, its main chain adopting a β-hairpin structure that is linked by two disulfide bridges. We report on the immune modulatory activity of PG-1 and its analogs in neutralizing bacterial endotoxin and capsular polysaccharides, consequently inhibiting inflammatory mediators’ release from macrophages. We demonstrate that the β-hairpin structure motif stabilized with at least one disulfide bridge is a prerequisite for the immune modulatory activity of this type of AMP. MDPI 2014-11-27 /pmc/articles/PMC4472440/ /pubmed/26097747 http://dx.doi.org/10.3390/antibiotics3040694 Text en © 2014 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Zughaier, Susu M. Svoboda, Pavel Pohl, Jan Structure-Dependent Immune Modulatory Activity of Protegrin-1 Analogs |
title | Structure-Dependent Immune Modulatory Activity of Protegrin-1 Analogs |
title_full | Structure-Dependent Immune Modulatory Activity of Protegrin-1 Analogs |
title_fullStr | Structure-Dependent Immune Modulatory Activity of Protegrin-1 Analogs |
title_full_unstemmed | Structure-Dependent Immune Modulatory Activity of Protegrin-1 Analogs |
title_short | Structure-Dependent Immune Modulatory Activity of Protegrin-1 Analogs |
title_sort | structure-dependent immune modulatory activity of protegrin-1 analogs |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4472440/ https://www.ncbi.nlm.nih.gov/pubmed/26097747 http://dx.doi.org/10.3390/antibiotics3040694 |
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