The rapid increase in the incidence of multidrug-resistant
infections today has led to enormous interest in
antimicrobial peptides (AMPs) as suitable compounds for developing unusual
antibiotics. In this study,
clavanin A, an
antimicrobial peptide previously isolated from the marine tunicate Styela clava, was selected as a purposeful molecule that could be used in controlling
infection and further synthesized.
Clavanin A was in vitro evaluated against Staphylococcus aureus and Escherichia coli as well as toward L929 mouse fibroblasts and skin primary cells (SPCs). Moreover, this
peptide was challenged here in an in vivo
wound and
sepsis model, and the immune response was also analyzed. Despite displaying clear in vitro antimicrobial activity toward Gram-positive and -negative bacteria,
clavanin A showed no cytotoxic activities against mammalian cells, and in acute toxicity tests, no adverse reaction was observed at any of the concentrations. Moreover,
clavanin A significantly reduced the S. aureus CFU in an experimental
wound model. This
peptide also reduced the mortality of mice infected with E. coli and S. aureus by 80% compared with that of control animals (treated with
phosphate-buffered saline [PBS]): these data suggest that
clavanin A prevents the start of
sepsis and thereby reduces mortality. These data suggest that
clavanin A is an
AMP that could improve the development of novel
peptide-based strategies for the treatment of
wound and
sepsis infections.