Structural and functional characterization of peptides derived from the carboxy‐terminal region of a defensin from the tick Ornithodoros savignyi. (31st March 2013)
- Record Type:
- Journal Article
- Title:
- Structural and functional characterization of peptides derived from the carboxy‐terminal region of a defensin from the tick Ornithodoros savignyi. (31st March 2013)
- Main Title:
- Structural and functional characterization of peptides derived from the carboxy‐terminal region of a defensin from the tick Ornithodoros savignyi
- Authors:
- Prinsloo, Lezaan
Naidoo, Alex
Serem, June
Taute, Helena
Sayed, Yasien
Bester, Megan
Neitz, Albert
Gaspar, Anabella - Abstract:
- <abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Tick defensins may serve as templates for the development of multifunctional peptides. The purpose of this study was to evaluate shorter peptides derived from tick defensin isoform 2 (OsDef2) in terms of their antibacterial, antioxidant, and cytotoxic activities. We compared the structural and functional properties of a synthetic peptide derived from the carboxy‐terminal of the parent peptide (Os) to that of an analogue in which the three cysteine residues were omitted (Os–C). Here, we report that both peptides were bactericidal (MBC values ranging from 0.94–15 µg/ml) to both Gram‐positive and Gram‐negative bacteria, whereas the parent peptide only exhibited Gram‐positive antibacterial activity. The Os peptide was found to be two‐fold more active than Os–C against three of the four tested bacteria but equally active against <italic>Staphylococcus aureus</italic>. Os showed rapid killing kinetics against both <italic>Escherichia coli</italic> and <italic>Bacillus subtilis</italic>, whereas Os–C took longer, suggesting different modes of action. Scanning electron microscopy showed that in contrast to melittin for which blebbing of bacterial surfaces was observed, cells exposed to either peptide appeared flattened and empty. Circular dichroism data indicated that in a membrane‐mimicking environment, the cysteine‐containing peptide has a higher <italic>α</italic>‐helical content. Both<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Tick defensins may serve as templates for the development of multifunctional peptides. The purpose of this study was to evaluate shorter peptides derived from tick defensin isoform 2 (OsDef2) in terms of their antibacterial, antioxidant, and cytotoxic activities. We compared the structural and functional properties of a synthetic peptide derived from the carboxy‐terminal of the parent peptide (Os) to that of an analogue in which the three cysteine residues were omitted (Os–C). Here, we report that both peptides were bactericidal (MBC values ranging from 0.94–15 µg/ml) to both Gram‐positive and Gram‐negative bacteria, whereas the parent peptide only exhibited Gram‐positive antibacterial activity. The Os peptide was found to be two‐fold more active than Os–C against three of the four tested bacteria but equally active against <italic>Staphylococcus aureus</italic>. Os showed rapid killing kinetics against both <italic>Escherichia coli</italic> and <italic>Bacillus subtilis</italic>, whereas Os–C took longer, suggesting different modes of action. Scanning electron microscopy showed that in contrast to melittin for which blebbing of bacterial surfaces was observed, cells exposed to either peptide appeared flattened and empty. Circular dichroism data indicated that in a membrane‐mimicking environment, the cysteine‐containing peptide has a higher <italic>α</italic>‐helical content. Both peptides were found to be non‐toxic to mammalian cells. Moreover, the peptides displayed potent antioxidant activity and were 12 times more active than melittin. Multifunctional peptides hold potential for a wide range of clinical applications and further investigation into their mode of antibacterial and antioxidant properties is therefore warranted. Copyright © 2013 European Peptide Society and John Wiley &amp; Sons, Ltd.</p> </abstract> … (more)
- Is Part Of:
- Journal of peptide science. Volume 19:Number 5(2013:May)
- Journal:
- Journal of peptide science
- Issue:
- Volume 19:Number 5(2013:May)
- Issue Display:
- Volume 19, Issue 5 (2013)
- Year:
- 2013
- Volume:
- 19
- Issue:
- 5
- Issue Sort Value:
- 2013-0019-0005-0000
- Page Start:
- 325
- Page End:
- 332
- Publication Date:
- 2013-03-31
- Subjects:
- Peptides -- Periodicals
Peptides -- Periodicals
572.65 - Journal URLs:
- http://onlinelibrary.wiley.com/ ↗
- DOI:
- 10.1002/psc.2505 ↗
- Languages:
- English
- ISSNs:
- 1075-2617
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5030.530000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 3449.xml