dc.contributor.author |
Mbuayama, Kabuzi R.
|
|
dc.contributor.author |
Taute, Helena
|
|
dc.contributor.author |
Stromstedt, Adam A.
|
|
dc.contributor.author |
Bester, Megan Jean
|
|
dc.contributor.author |
Gaspar, Anabella Regina Marques
|
|
dc.date.accessioned |
2022-07-25T06:39:59Z |
|
dc.date.issued |
2022-05 |
|
dc.description |
Supporting Information: Table S1. Physicochemical properties and antifungal activity of OsDef2 derived peptides.
Figure S1. Effect of sodium azide on the intracellular translocation of 5-FAM penetratin. C. albicans cells were pre-incubated with 5mM NaN3 for 30 min and treated with 5-FAM penetratin. The cells were counterstained with DAPI (blue) and visualized by confocal microscopy. Scale bars are 10 μm.
Figure S2. DAPI stained images of 5-FAM-peptides in C. albicans. Cells were exposed for 50 min to 2.5 μM of 5-FAM-peptides, counterstained with DAPI (blue) and visualized by confocal microscopy. Top and bottom panel show same images at lower and higher magnification, respectively. Short arrow: fragmented nuclear DNA; long arrow: tubular-shaped DNA, in contrast to single and round nucleus observed in untreated cells. Images are representatives of three independent experiments, in duplicate. Scale bars are 10 μm. |
en_US |
dc.description.abstract |
Please read abstract in the article. |
en_US |
dc.description.department |
Anatomy |
en_US |
dc.description.department |
Biochemistry |
en_US |
dc.description.department |
Genetics |
en_US |
dc.description.department |
Microbiology and Plant Pathology |
en_US |
dc.description.embargo |
2022-12-05 |
|
dc.description.librarian |
hj2022 |
en_US |
dc.description.sponsorship |
University of Pretoria;
National Research Foundation;
South African Medical Research Council. |
en_US |
dc.description.uri |
http://wileyonlinelibrary.com/journal/psc |
en_US |
dc.identifier.citation |
Mbuayama, K.R., Taute, H., Stromstedt, A.A., Bester, M.J. & Gaspar, A.R.M. Antifungal activity and mode of action of synthetic peptides derived from the tick OsDef2 defensin. Journal of Peptide Science 2022;28(5):e3383.doi:10.1002/psc.3383. |
en_US |
dc.identifier.issn |
1075-2617 (print) |
|
dc.identifier.issn |
1099-1387 (online) |
|
dc.identifier.other |
10.1002/psc.3383 |
|
dc.identifier.uri |
https://repository.up.ac.za/handle/2263/86414 |
|
dc.language.iso |
en |
en_US |
dc.publisher |
Wiley |
en_US |
dc.rights |
© 2021 European Peptide Society and John Wiley & Sons, Ltd. This is the pre-peer reviewed version of the following article : Antifungal activity and mode of action of synthetic peptides derived from the tick OsDef2 defensin. Journal of Peptide Science 2022;28(5):e3383.doi:10.1002/psc.3383, which has been published in final form at : http://wileyonlinelibrary.com/journal/psc. |
en_US |
dc.subject |
Antimicrobial peptides |
en_US |
dc.subject |
Defensins |
en_US |
dc.subject |
Membrane permeabilization |
en_US |
dc.subject |
Reactive oxygen species (ROS) |
en_US |
dc.subject |
Ticks |
en_US |
dc.title |
Antifungal activity and mode of action of synthetic peptides derived from the tick OsDef2 defensin |
en_US |
dc.type |
Postprint Article |
en_US |