Chlorhexidine: beta-cyclodextrin inhibits yeast growth by extraction of ergosterol
Autor(a) principal: | |
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Data de Publicação: | 2012 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Brazilian Journal of Microbiology |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822012000200047 |
Resumo: | Chlorhexidine (Cx) augmented with beta-cyclodextrin (β-cd) inclusion compounds, termed Cx:β-cd complexes, have been developed for use as antiseptic agents. The aim of this study was to examine the interactions of Cx:β-cd complexes, prepared at different molecular ratios, with sterol and yeast membranes. The Minimal Inhibitory Concentration (MIC) against the yeast Candida albicans (C.a.) was determined for each complex; the MICs were found to range from 0.5 to 2 µg/mL. To confirm the MIC data, quantitative analysis of viable cells was performed using trypan blue staining. Mechanistic characterization of the interactions that the Cx:β-cd complexes have with the yeast membrane and assessment of membrane morphology following exposure to Cx:β-cd complexes were performed using Sterol Quantification Method analysis (SQM) and scanning electron microscopy (SEM). SQM revealed that sterol extraction increased with increasing β-cd concentrations (1.71 × 10³; 1.4 × 10³; 3.45 × 10³, and 3.74 × 10³ CFU for 1:1, 1:2, 1:3, and 1:4, respectively), likely as a consequence of membrane ergosterol solubilization. SEM images demonstrated that cell membrane damage is a visible and significant mechanism that contributes to the antimicrobial effects of Cx:β-cd complexes. Cell disorganization increased significantly as the proportion of β-cyclodextrin present in the complex increased. Morphology of cells exposed to complexes with 1:3 and 1:4 molar ratios of Cx:β-cd were observed to have large aggregates mixed with yeast remains, representing more membrane disruption than that observed in cells treated with Cx alone. In conclusion, nanoaggregates of Cx:β-cd complexes block yeast growth via ergosterol extraction, permeabilizing the membrane by creating cluster-like structures within the cell membrane, possibly due to high amounts of hydrogen bonding. |
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Brazilian Journal of Microbiology |
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Chlorhexidine: beta-cyclodextrin inhibits yeast growth by extraction of ergosterolChlorhexidineβ-cyclodextrinmembrane-drug interactionsChlorhexidine (Cx) augmented with beta-cyclodextrin (β-cd) inclusion compounds, termed Cx:β-cd complexes, have been developed for use as antiseptic agents. The aim of this study was to examine the interactions of Cx:β-cd complexes, prepared at different molecular ratios, with sterol and yeast membranes. The Minimal Inhibitory Concentration (MIC) against the yeast Candida albicans (C.a.) was determined for each complex; the MICs were found to range from 0.5 to 2 µg/mL. To confirm the MIC data, quantitative analysis of viable cells was performed using trypan blue staining. Mechanistic characterization of the interactions that the Cx:β-cd complexes have with the yeast membrane and assessment of membrane morphology following exposure to Cx:β-cd complexes were performed using Sterol Quantification Method analysis (SQM) and scanning electron microscopy (SEM). SQM revealed that sterol extraction increased with increasing β-cd concentrations (1.71 × 10³; 1.4 × 10³; 3.45 × 10³, and 3.74 × 10³ CFU for 1:1, 1:2, 1:3, and 1:4, respectively), likely as a consequence of membrane ergosterol solubilization. SEM images demonstrated that cell membrane damage is a visible and significant mechanism that contributes to the antimicrobial effects of Cx:β-cd complexes. Cell disorganization increased significantly as the proportion of β-cyclodextrin present in the complex increased. Morphology of cells exposed to complexes with 1:3 and 1:4 molar ratios of Cx:β-cd were observed to have large aggregates mixed with yeast remains, representing more membrane disruption than that observed in cells treated with Cx alone. In conclusion, nanoaggregates of Cx:β-cd complexes block yeast growth via ergosterol extraction, permeabilizing the membrane by creating cluster-like structures within the cell membrane, possibly due to high amounts of hydrogen bonding.Sociedade Brasileira de Microbiologia2012-06-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822012000200047Brazilian Journal of Microbiology v.43 n.2 2012reponame:Brazilian Journal of Microbiologyinstname:Sociedade Brasileira de Microbiologia (SBM)instacron:SBM10.1590/S1517-83822012000200047info:eu-repo/semantics/openAccessTeixeira,K. I. R.Araújo,P. V.Sinisterra,R. D.Cortés,M. E.eng2012-08-07T00:00:00Zoai:scielo:S1517-83822012000200047Revistahttps://www.scielo.br/j/bjm/ONGhttps://old.scielo.br/oai/scielo-oai.phpbjm@sbmicrobiologia.org.br||mbmartin@usp.br1678-44051517-8382opendoar:2012-08-07T00:00Brazilian Journal of Microbiology - Sociedade Brasileira de Microbiologia (SBM)false |
dc.title.none.fl_str_mv |
Chlorhexidine: beta-cyclodextrin inhibits yeast growth by extraction of ergosterol |
title |
Chlorhexidine: beta-cyclodextrin inhibits yeast growth by extraction of ergosterol |
spellingShingle |
Chlorhexidine: beta-cyclodextrin inhibits yeast growth by extraction of ergosterol Teixeira,K. I. R. Chlorhexidine β-cyclodextrin membrane-drug interactions |
title_short |
Chlorhexidine: beta-cyclodextrin inhibits yeast growth by extraction of ergosterol |
title_full |
Chlorhexidine: beta-cyclodextrin inhibits yeast growth by extraction of ergosterol |
title_fullStr |
Chlorhexidine: beta-cyclodextrin inhibits yeast growth by extraction of ergosterol |
title_full_unstemmed |
Chlorhexidine: beta-cyclodextrin inhibits yeast growth by extraction of ergosterol |
title_sort |
Chlorhexidine: beta-cyclodextrin inhibits yeast growth by extraction of ergosterol |
author |
Teixeira,K. I. R. |
author_facet |
Teixeira,K. I. R. Araújo,P. V. Sinisterra,R. D. Cortés,M. E. |
author_role |
author |
author2 |
Araújo,P. V. Sinisterra,R. D. Cortés,M. E. |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Teixeira,K. I. R. Araújo,P. V. Sinisterra,R. D. Cortés,M. E. |
dc.subject.por.fl_str_mv |
Chlorhexidine β-cyclodextrin membrane-drug interactions |
topic |
Chlorhexidine β-cyclodextrin membrane-drug interactions |
description |
Chlorhexidine (Cx) augmented with beta-cyclodextrin (β-cd) inclusion compounds, termed Cx:β-cd complexes, have been developed for use as antiseptic agents. The aim of this study was to examine the interactions of Cx:β-cd complexes, prepared at different molecular ratios, with sterol and yeast membranes. The Minimal Inhibitory Concentration (MIC) against the yeast Candida albicans (C.a.) was determined for each complex; the MICs were found to range from 0.5 to 2 µg/mL. To confirm the MIC data, quantitative analysis of viable cells was performed using trypan blue staining. Mechanistic characterization of the interactions that the Cx:β-cd complexes have with the yeast membrane and assessment of membrane morphology following exposure to Cx:β-cd complexes were performed using Sterol Quantification Method analysis (SQM) and scanning electron microscopy (SEM). SQM revealed that sterol extraction increased with increasing β-cd concentrations (1.71 × 10³; 1.4 × 10³; 3.45 × 10³, and 3.74 × 10³ CFU for 1:1, 1:2, 1:3, and 1:4, respectively), likely as a consequence of membrane ergosterol solubilization. SEM images demonstrated that cell membrane damage is a visible and significant mechanism that contributes to the antimicrobial effects of Cx:β-cd complexes. Cell disorganization increased significantly as the proportion of β-cyclodextrin present in the complex increased. Morphology of cells exposed to complexes with 1:3 and 1:4 molar ratios of Cx:β-cd were observed to have large aggregates mixed with yeast remains, representing more membrane disruption than that observed in cells treated with Cx alone. In conclusion, nanoaggregates of Cx:β-cd complexes block yeast growth via ergosterol extraction, permeabilizing the membrane by creating cluster-like structures within the cell membrane, possibly due to high amounts of hydrogen bonding. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012-06-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822012000200047 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822012000200047 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S1517-83822012000200047 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Sociedade Brasileira de Microbiologia |
publisher.none.fl_str_mv |
Sociedade Brasileira de Microbiologia |
dc.source.none.fl_str_mv |
Brazilian Journal of Microbiology v.43 n.2 2012 reponame:Brazilian Journal of Microbiology instname:Sociedade Brasileira de Microbiologia (SBM) instacron:SBM |
instname_str |
Sociedade Brasileira de Microbiologia (SBM) |
instacron_str |
SBM |
institution |
SBM |
reponame_str |
Brazilian Journal of Microbiology |
collection |
Brazilian Journal of Microbiology |
repository.name.fl_str_mv |
Brazilian Journal of Microbiology - Sociedade Brasileira de Microbiologia (SBM) |
repository.mail.fl_str_mv |
bjm@sbmicrobiologia.org.br||mbmartin@usp.br |
_version_ |
1752122204662792192 |