Antibiotics (Nov 2014)

Structure-Dependent Immune Modulatory Activity of Protegrin-1 Analogs

  • Susu M. Zughaier,
  • Pavel Svoboda,
  • Jan Pohl

DOI
https://doi.org/10.3390/antibiotics3040694
Journal volume & issue
Vol. 3, no. 4
pp. 694 – 713

Abstract

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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.

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