Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Zughaier, Susu M., Svoboda, Pavel, Pohl, Jan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2014
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
_version_ 1782377057052786688
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
work_keys_str_mv AT zughaiersusum structuredependentimmunemodulatoryactivityofprotegrin1analogs
AT svobodapavel structuredependentimmunemodulatoryactivityofprotegrin1analogs
AT pohljan structuredependentimmunemodulatoryactivityofprotegrin1analogs