Anti-inflammatory and anti-endotoxin properties of peptides derived from the carboxy-terminal region of a defensin from the tick Ornithodoros savignyi
Anti-inflammatory and anti-endotoxin properties of peptides derived from the carboxy-terminal region of a defensin from the tick Ornithodoros savignyi
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DOI：
10.1002/psc.2838
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发表时间：
2016-01-01
影响因子：
2.1
通讯作者：
Gaspar, Anabella R. M.
中科院分区：
文献类型：
--
作者：
Malan, Melissa;Serem, June C.;Gaspar, Anabella R. M.
Antimicrobial peptides are small cationic peptides that possess a large spectrum of bioactivities, including antimicrobial, anti-inflammatory and antioxidant activities. Several antimicrobial peptides are known to inhibit lipopolysaccharide (LPS)-induced inflammation in vitro and to protect animals from sepsis. In this study, the cellular anti-inflammatory and anti-endotoxin activities of Os and Os-C, peptides derived from the carboxy-terminal of a tick defensin, were investigated. Both Os and Os-C were found to bind LPS in vitro, albeit to a lesser extent than polymyxin B and melittin, known endotoxin-binding peptides. Binding to LPS was found to reduce the bactericidal activity of Os and Os-C against Escherichia coli confirming the affinity of both peptides for LPS. At a concentration of 25 mu M, the nitric oxide (NO) scavenging activity of Os was higher than glutathione, a known NO scavenger. In contrast, Os-C showed no scavenging activity. Os and Os-C inhibited LPS/IFN- induced NO and TNF- production in RAW 264.7 cells in a concentration-dependent manner, with no cellular toxicity even at a concentration of 100 mu M. Although inhibition of NO and TNF- secretion was more pronounced for melittin and polymyxin B, significant cytotoxicity was observed at concentrations of 1.56 mu M and 25 mu M for melittin and polymyxin B, respectively. In addition, Os, Os-C and glutathione protected RAW 264.7 cells from oxidative damage at concentrations as low as 25 mu M. This study identified that besides previously reported antibacterial activity of Os and Os-C, both peptides have in addition anti-inflammatory and anti-endotoxin properties. Copyright (c) 2015 European Peptide Society and John Wiley & Sons, Ltd.
