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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dc.contributor.author Malan, Melissa
dc.contributor.author Serem, June Cheptoo
dc.contributor.author Bester, Megan Jean
dc.contributor.author Neitz, A.W.H. (Albert Walter Herman)
dc.contributor.author Gaspar, A.R.M. (Anabella Regina Marques)
dc.date.accessioned 2016-03-11T09:04:14Z
dc.date.issued 2016-01
dc.description.abstract Antimicrobial peptides (AMPs) are small, cationic peptides that possess a large spectrum of bioactivities, including antimicrobial, anti-inflammatory and antioxidant activities. Several AMPs 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 (OsDef2), 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 μM, the nitric oxide (NO) scavenging activity of Os was higher than glutathione (GSH), a known NO scavenger. In contrast, Os-C showed no scavenging activity. Os and Os-C inhibited LPS/IFN-γ induced NO and TNF-α production in RAW 264.7 cells in a concentration-dependent manner, with no cellular toxicity even at a concentration of 100 μM. Although inhibition of NO and TNF-α secretion was more pronounced for melittin and polymyxin B, significant cytotoxicity was observed at concentrations of 1.56 μM and 25 μM for melittin and polymyxin B, respectively. In addition, Os, Os-C and GSH protected RAW 264.7 cells from oxidative damage at concentrations as low as 25 μM. 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. en_ZA
dc.description.embargo 2017-01-31
dc.description.librarian hb2015 en_ZA
dc.description.sponsorship Medical Research Council (MRC), the National Research Foundation (NRF) of South Africa and the University of Pretoria. en_ZA
dc.description.uri http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1099-1387 en_ZA
dc.identifier.citation Malan, M, Serem, JC, Bester, MJ, Neitz, AWH & Gaspar, ARM 2016, 'Anti-inflammatory and anti-endotoxin properties of peptides derived from the carboxy-terminal region of a defensin from the tick Ornithodoros savignyi', Journal of Peptide Science, vol. 22, no. 1, pp. 43-51. en_ZA
dc.identifier.issn 1075-2617 (print)
dc.identifier.issn 1099-1387 (online)
dc.identifier.other 10.1002/psc.2838
dc.identifier.uri http://hdl.handle.net/2263/51800
dc.language.iso en en_ZA
dc.publisher Wiley en_ZA
dc.rights © European Peptide Society and John Wiley & Sons, Ltd. The definite version is available at : http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1099-1387. en_ZA
dc.subject Sepsis en_ZA
dc.subject Defensin en_ZA
dc.subject Tick en_ZA
dc.subject Anti-inflammatory en_ZA
dc.subject Anti-endotoxin en_ZA
dc.subject Antioxidant en_ZA
dc.subject NO scavenging en_ZA
dc.subject Antimicrobial peptide (AMP) en_ZA
dc.subject Lipopolysaccharide (LPS) en_ZA
dc.title Anti-inflammatory and anti-endotoxin properties of peptides derived from the carboxy-terminal region of a defensin from the tick Ornithodoros savignyi en_ZA
dc.type Postprint Article en_ZA


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