Please note that UPSpace will be unavailable from Friday, 2 May at 18:00 (South African Time) until Sunday, 4 May at 20:00 due to scheduled system upgrades. We apologise for any inconvenience this may cause and appreciate your understanding.
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 |