Structure-Dependent Immune Modulatory Activity of Protegrin-1 Analogs
AbstractProtegrins 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. View Full-Text
Scifeed alert for new publicationsNever miss any articles matching your research from any publisher
- Get alerts for new papers matching your research
- Find out the new papers from selected authors
- Updated daily for 49'000+ journals and 6000+ publishers
- Define your Scifeed now
Zughaier, S.M.; Svoboda, P.; Pohl, J. Structure-Dependent Immune Modulatory Activity of Protegrin-1 Analogs. Antibiotics 2014, 3, 694-713.
Zughaier SM, Svoboda P, Pohl J. Structure-Dependent Immune Modulatory Activity of Protegrin-1 Analogs. Antibiotics. 2014; 3(4):694-713.Chicago/Turabian Style
Zughaier, Susu M.; Svoboda, Pavel; Pohl, Jan. 2014. "Structure-Dependent Immune Modulatory Activity of Protegrin-1 Analogs." Antibiotics 3, no. 4: 694-713.