The antiproliferative peptide Ctn[15-34] is active against multidrug-resistant yeasts and Candida albicans and C. neoforms
Autor(a) principal: | |
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Data de Publicação: | 2019 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da Universidade Federal do Ceará (UFC) |
Texto Completo: | http://www.repositorio.ufc.br/handle/riufc/59701 |
Resumo: | ims: Crotalicidin (Ctn), a cathelicidin-related antimicrobial peptide from theSouth American rattlesnake venom gland, and its C-terminal Ctn[15-34] fragment,have exhibited important activities against micro-organisms, trypanosomatidprotozoa and certain lines of tumour cells. Herein, the activity against clinicalstrains of fluconazole-resistant Candida albicans and of amphotericin B andfluconazole-resistant Cryptococcus neoformans was investigated.Methods and Results: Microdilution and luminescent cell viability tests wereused to evaluate and compare the susceptibility of pathogenic yeasts to thesepeptides. The time–kill curves of the most active Ctn[15-34] alone or incombination with fluconazole against drug-resistant yeasts were determined.Concomitantly, the fungicidal and/or fungistatic effects of Ctn[15-34] werevisualized by the spotting test. The peptides were active against all strains,including those resistant to antifungal agents. The association of fluconazolewith both Ctn and Ctn[15-34], although not synergic, was additive. Incontrast, such pattern was not observed for C. neoformans.Conclusions: Overall, Ctn and Ctn[15-34] are potential antifungal leadsdisplaying anti-yeast activities against clinical isolates endowed with drugresistance mechanisms.Significance and Impact of the Study: The effective peptide activity againstresistant strains of pathogenic yeasts demonstrates that crotalicidin-derivedpeptides are promising templates to develop new antifungal pharmaceuthicals |
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The antiproliferative peptide Ctn[15-34] is active against multidrug-resistant yeasts and Candida albicans and C. neoformsThe antiproliferative peptide Ctn[15-34] is active against multidrug-resistant yeasts and Candida albicans and C. neoformsAntimicrobianoResistênciaFármacosims: Crotalicidin (Ctn), a cathelicidin-related antimicrobial peptide from theSouth American rattlesnake venom gland, and its C-terminal Ctn[15-34] fragment,have exhibited important activities against micro-organisms, trypanosomatidprotozoa and certain lines of tumour cells. Herein, the activity against clinicalstrains of fluconazole-resistant Candida albicans and of amphotericin B andfluconazole-resistant Cryptococcus neoformans was investigated.Methods and Results: Microdilution and luminescent cell viability tests wereused to evaluate and compare the susceptibility of pathogenic yeasts to thesepeptides. The time–kill curves of the most active Ctn[15-34] alone or incombination with fluconazole against drug-resistant yeasts were determined.Concomitantly, the fungicidal and/or fungistatic effects of Ctn[15-34] werevisualized by the spotting test. The peptides were active against all strains,including those resistant to antifungal agents. The association of fluconazolewith both Ctn and Ctn[15-34], although not synergic, was additive. Incontrast, such pattern was not observed for C. neoformans.Conclusions: Overall, Ctn and Ctn[15-34] are potential antifungal leadsdisplaying anti-yeast activities against clinical isolates endowed with drugresistance mechanisms.Significance and Impact of the Study: The effective peptide activity againstresistant strains of pathogenic yeasts demonstrates that crotalicidin-derivedpeptides are promising templates to develop new antifungal pharmaceuthicalsJournal Of Applied Microbiology2021-07-23T11:22:04Z2021-07-23T11:22:04Z2019info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfAGUIAR, Francisca Lidiane Linhares de; CAVALCANTE, Carolina Sidrim de Paula; FONTENELLE, Raquel Oliveira dos Santos; FALCÃO, Cláudio Borges; ANDREU, David; RÁDIS-BAPTISTA, Gandhi. The antiproliferative peptide Ctn[15-34] is active against multidrug-resistant yeasts and Candida albicans and C. Neoforms Journal Of Applied Microbiology, United States, v. 10, 2019.1364-5072http://www.repositorio.ufc.br/handle/riufc/59701Aguiar, Francisca Lidiane Linhares deCavalcante, Carolina Sidrim De PaulaFontenelle, Raquel Oliveira dos SantosFalcão, Cláudio BorgesAndreu, DavidRádis-Baptista, Gandhiengreponame:Repositório Institucional da Universidade Federal do Ceará (UFC)instname:Universidade Federal do Ceará (UFC)instacron:UFCinfo:eu-repo/semantics/openAccess2022-11-30T14:04:26Zoai:repositorio.ufc.br:riufc/59701Repositório InstitucionalPUBhttp://www.repositorio.ufc.br/ri-oai/requestbu@ufc.br || repositorio@ufc.bropendoar:2024-09-11T18:36:15.086083Repositório Institucional da Universidade Federal do Ceará (UFC) - Universidade Federal do Ceará (UFC)false |
dc.title.none.fl_str_mv |
The antiproliferative peptide Ctn[15-34] is active against multidrug-resistant yeasts and Candida albicans and C. neoforms The antiproliferative peptide Ctn[15-34] is active against multidrug-resistant yeasts and Candida albicans and C. neoforms |
title |
The antiproliferative peptide Ctn[15-34] is active against multidrug-resistant yeasts and Candida albicans and C. neoforms |
spellingShingle |
The antiproliferative peptide Ctn[15-34] is active against multidrug-resistant yeasts and Candida albicans and C. neoforms Aguiar, Francisca Lidiane Linhares de Antimicrobiano Resistência Fármacos |
title_short |
The antiproliferative peptide Ctn[15-34] is active against multidrug-resistant yeasts and Candida albicans and C. neoforms |
title_full |
The antiproliferative peptide Ctn[15-34] is active against multidrug-resistant yeasts and Candida albicans and C. neoforms |
title_fullStr |
The antiproliferative peptide Ctn[15-34] is active against multidrug-resistant yeasts and Candida albicans and C. neoforms |
title_full_unstemmed |
The antiproliferative peptide Ctn[15-34] is active against multidrug-resistant yeasts and Candida albicans and C. neoforms |
title_sort |
The antiproliferative peptide Ctn[15-34] is active against multidrug-resistant yeasts and Candida albicans and C. neoforms |
author |
Aguiar, Francisca Lidiane Linhares de |
author_facet |
Aguiar, Francisca Lidiane Linhares de Cavalcante, Carolina Sidrim De Paula Fontenelle, Raquel Oliveira dos Santos Falcão, Cláudio Borges Andreu, David Rádis-Baptista, Gandhi |
author_role |
author |
author2 |
Cavalcante, Carolina Sidrim De Paula Fontenelle, Raquel Oliveira dos Santos Falcão, Cláudio Borges Andreu, David Rádis-Baptista, Gandhi |
author2_role |
author author author author author |
dc.contributor.author.fl_str_mv |
Aguiar, Francisca Lidiane Linhares de Cavalcante, Carolina Sidrim De Paula Fontenelle, Raquel Oliveira dos Santos Falcão, Cláudio Borges Andreu, David Rádis-Baptista, Gandhi |
dc.subject.por.fl_str_mv |
Antimicrobiano Resistência Fármacos |
topic |
Antimicrobiano Resistência Fármacos |
description |
ims: Crotalicidin (Ctn), a cathelicidin-related antimicrobial peptide from theSouth American rattlesnake venom gland, and its C-terminal Ctn[15-34] fragment,have exhibited important activities against micro-organisms, trypanosomatidprotozoa and certain lines of tumour cells. Herein, the activity against clinicalstrains of fluconazole-resistant Candida albicans and of amphotericin B andfluconazole-resistant Cryptococcus neoformans was investigated.Methods and Results: Microdilution and luminescent cell viability tests wereused to evaluate and compare the susceptibility of pathogenic yeasts to thesepeptides. The time–kill curves of the most active Ctn[15-34] alone or incombination with fluconazole against drug-resistant yeasts were determined.Concomitantly, the fungicidal and/or fungistatic effects of Ctn[15-34] werevisualized by the spotting test. The peptides were active against all strains,including those resistant to antifungal agents. The association of fluconazolewith both Ctn and Ctn[15-34], although not synergic, was additive. Incontrast, such pattern was not observed for C. neoformans.Conclusions: Overall, Ctn and Ctn[15-34] are potential antifungal leadsdisplaying anti-yeast activities against clinical isolates endowed with drugresistance mechanisms.Significance and Impact of the Study: The effective peptide activity againstresistant strains of pathogenic yeasts demonstrates that crotalicidin-derivedpeptides are promising templates to develop new antifungal pharmaceuthicals |
publishDate |
2019 |
dc.date.none.fl_str_mv |
2019 2021-07-23T11:22:04Z 2021-07-23T11:22:04Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
AGUIAR, Francisca Lidiane Linhares de; CAVALCANTE, Carolina Sidrim de Paula; FONTENELLE, Raquel Oliveira dos Santos; FALCÃO, Cláudio Borges; ANDREU, David; RÁDIS-BAPTISTA, Gandhi. The antiproliferative peptide Ctn[15-34] is active against multidrug-resistant yeasts and Candida albicans and C. Neoforms Journal Of Applied Microbiology, United States, v. 10, 2019. 1364-5072 http://www.repositorio.ufc.br/handle/riufc/59701 |
identifier_str_mv |
AGUIAR, Francisca Lidiane Linhares de; CAVALCANTE, Carolina Sidrim de Paula; FONTENELLE, Raquel Oliveira dos Santos; FALCÃO, Cláudio Borges; ANDREU, David; RÁDIS-BAPTISTA, Gandhi. The antiproliferative peptide Ctn[15-34] is active against multidrug-resistant yeasts and Candida albicans and C. Neoforms Journal Of Applied Microbiology, United States, v. 10, 2019. 1364-5072 |
url |
http://www.repositorio.ufc.br/handle/riufc/59701 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Journal Of Applied Microbiology |
publisher.none.fl_str_mv |
Journal Of Applied Microbiology |
dc.source.none.fl_str_mv |
reponame:Repositório Institucional da Universidade Federal do Ceará (UFC) instname:Universidade Federal do Ceará (UFC) instacron:UFC |
instname_str |
Universidade Federal do Ceará (UFC) |
instacron_str |
UFC |
institution |
UFC |
reponame_str |
Repositório Institucional da Universidade Federal do Ceará (UFC) |
collection |
Repositório Institucional da Universidade Federal do Ceará (UFC) |
repository.name.fl_str_mv |
Repositório Institucional da Universidade Federal do Ceará (UFC) - Universidade Federal do Ceará (UFC) |
repository.mail.fl_str_mv |
bu@ufc.br || repositorio@ufc.br |
_version_ |
1813028872844738560 |