title: Structure-Dependent Immune Modulatory Activity of Protegrin-1 Analogs.
abstract: 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.
authors.affiliation: Department of Microbiology and Immunology, Emory University School of Medicine, Atlanta, GA 30322, USA ; Laboratories of Microbial Pathogenesis, Atlanta Department of Veterans Affairs Medical Center, Atlanta, GA 30033, USA.
authors.forename: Susu M
authors.initials: SM
authors.lastname: Zughaier
authors.affiliation: Microchemical and Proteomics Facility, Emory University School of Medicine, Atlanta, GA 30322, USA ; Biotechnology Core Facility Branch, Division of Scientific Resources, Centers for Disease Control and Prevention, Atlanta, GA 30333, USA.
authors.forename: Pavel
authors.initials: P
authors.lastname: Svoboda
authors.affiliation: Microchemical and Proteomics Facility, Emory University School of Medicine, Atlanta, GA 30322, USA ; Biotechnology Core Facility Branch, Division of Scientific Resources, Centers for Disease Control and Prevention, Atlanta, GA 30333, USA.
authors.forename: Jan
authors.initials: J
authors.lastname: Pohl
keywords: Toll-like receptor (TLR) ligands; cytokines; innate immunity; macrophage; protegrin-1 (PG-1)