title: Antimicrobial activity of a C-terminal peptide from human extracellular superoxide dismutase.
abstract: BACKGROUND
  Antimicrobial peptides (AMP) are important effectors of the innate immune system. Although there is increasing evidence that AMPs influence bacteria in a multitude of ways, bacterial wall rupture plays the pivotal role in the bactericidal action of AMPs. Structurally, AMPs share many similarities with endogenous heparin-binding peptides with respect to secondary structure, cationicity, and amphipathicity.
  
  
  RESULTS
  In this study, we show that RQA21 (RQAREHSERKKRRRESECKAA), a cationic and hydrophilic heparin-binding peptide corresponding to the C-terminal region of extracellular superoxide dismutase (SOD), exerts antimicrobial activity against Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, Bacillus subtilis and Candida albicans. The peptide was also found to induce membrane leakage of negatively charged liposomes. However, its antibacterial effects were abrogated in physiological salt conditions as well as in plasma.
  
  
  CONCLUSIONS
  The results provide further evidence that heparin-binding peptide regions are multifunctional, but also illustrate that cationicity alone is not sufficient for AMP function at physiological conditions. However, our observation, apart from providing a link between heparin-binding peptides and AMPs, raises the hypothesis that proteolytically generated C-terminal SOD-derived peptides could interact with, and possibly counteract bacteria. Further studies are therefore merited to study a possible role of SOD in host defence.
authors: Division of Dermatology and Venereology, Department of Clinical Sciences, Biomedical Center B14, Lund University, Tornavägen 10, SE-22184 Lund, Sweden. mukesh.pasupuleti@med.lu.se
authors: Mukesh
authors: M
authors: Pasupuleti
authors: Mina
authors: M
authors: Davoudi
authors: Martin
authors: M
authors: Malmsten
authors: Artur
authors: A
authors: Schmidtchen