The inhibition of Candida albicans secreted aspartyl proteinase by triangular gold nanoparticles

Objective(s): The aim of this study was to synthesize triangular gold nanoparticles, and then to evaluate their capability for inhibition of Candida albicans secreted aspartyl proteinase 2(Sap2). Materials and Methods: To synthesize the nanoparticles, hydrogen tetrachloroaurate and hexadecyl trimeth...

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Main Authors: Farzaneh Haji Esmaeil Hajjar, Ali Jebali, Seyedhossein Hekmatimoghaddam
Format: Article
Language:English
Published: Mashhad University of Medical Sciences 2015-01-01
Series:Nanomedicine Journal
Subjects:
Online Access:http://nmj.mums.ac.ir/pdf_3469_2c9dfb42ef4f6d96540623e1c5a151c4.html
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spelling doaj-e5705c2890cb491dba8d04192748a0ba2020-11-25T02:29:37ZengMashhad University of Medical SciencesNanomedicine Journal2322-30492322-59042015-01-012154593469The inhibition of Candida albicans secreted aspartyl proteinase by triangular gold nanoparticlesFarzaneh Haji Esmaeil Hajjar0Ali Jebali1Seyedhossein Hekmatimoghaddam2Departments of Microbiology, Pars Hospital Lab, Tehran, Iran2Department of Genetics, Research and Clinical Center for Infertility, Shahid Sadoughi University of Medical Sciences, Yazd, Iran3Department of Laboratory Sciences, School of Paramedicine, Shahid Sadoughi University of Medical Sciences, Yazd, IranObjective(s): The aim of this study was to synthesize triangular gold nanoparticles, and then to evaluate their capability for inhibition of Candida albicans secreted aspartyl proteinase 2(Sap2). Materials and Methods: To synthesize the nanoparticles, hydrogen tetrachloroaurate and hexadecyl trimethyl ammonium bromide were incubated in presence of Sn(IV) meso-tetra(N-methyl-4-pyridyl) porphine tetratosylate chloride, and then characterized. Next, thirty clinical isolates of Candida albicans were obtained from patients suffering from vaginal candidiasis. Each Candida albicans isolate was first cultured in YCB-BSA medium, incubated for 24 h at 35 ºC. Then, 100 µL of triangular gold nanoparticles at three concentrations (16, 32, and 64 µg/mL) were added to Candida suspension, and incubated for 24 and 48 h at 35 ºC. To evaluate Sap activity, 0.1 mL of medium and 0.4 mL of 0.1 M sodium citrate buffer (pH 3.2) containing BSA 1% w/v were added, and incubated 15 minutes at 37 ºC. Then, the optical density of each tube was read at 280 nm. Enzyme activity was expressed as the amount (µM) of tyrosine equivalents released per min per ml of culture supernatant. Results: This study showed that the size of the nanoparticles was 70±50 nm. Sap activity evaluation demonstrated triangular gold nanoparticles could inhibit the enzyme, and the higher incubation time and concentration led to more decrease of Sap activity. Conclusion:For the first time, we demonstrated triangular gold nanoparticles as a novel inhibitor of Sap enzyme which may be useful for treatment of candidiasis.  http://nmj.mums.ac.ir/pdf_3469_2c9dfb42ef4f6d96540623e1c5a151c4.htmlCandida albicansPeptide ligandSecreted aspartyl proteinaseTriangular gold nanoparticles
collection DOAJ
language English
format Article
sources DOAJ
author Farzaneh Haji Esmaeil Hajjar
Ali Jebali
Seyedhossein Hekmatimoghaddam
spellingShingle Farzaneh Haji Esmaeil Hajjar
Ali Jebali
Seyedhossein Hekmatimoghaddam
The inhibition of Candida albicans secreted aspartyl proteinase by triangular gold nanoparticles
Nanomedicine Journal
Candida albicans
Peptide ligand
Secreted aspartyl proteinase
Triangular gold nanoparticles
author_facet Farzaneh Haji Esmaeil Hajjar
Ali Jebali
Seyedhossein Hekmatimoghaddam
author_sort Farzaneh Haji Esmaeil Hajjar
title The inhibition of Candida albicans secreted aspartyl proteinase by triangular gold nanoparticles
title_short The inhibition of Candida albicans secreted aspartyl proteinase by triangular gold nanoparticles
title_full The inhibition of Candida albicans secreted aspartyl proteinase by triangular gold nanoparticles
title_fullStr The inhibition of Candida albicans secreted aspartyl proteinase by triangular gold nanoparticles
title_full_unstemmed The inhibition of Candida albicans secreted aspartyl proteinase by triangular gold nanoparticles
title_sort inhibition of candida albicans secreted aspartyl proteinase by triangular gold nanoparticles
publisher Mashhad University of Medical Sciences
series Nanomedicine Journal
issn 2322-3049
2322-5904
publishDate 2015-01-01
description Objective(s): The aim of this study was to synthesize triangular gold nanoparticles, and then to evaluate their capability for inhibition of Candida albicans secreted aspartyl proteinase 2(Sap2). Materials and Methods: To synthesize the nanoparticles, hydrogen tetrachloroaurate and hexadecyl trimethyl ammonium bromide were incubated in presence of Sn(IV) meso-tetra(N-methyl-4-pyridyl) porphine tetratosylate chloride, and then characterized. Next, thirty clinical isolates of Candida albicans were obtained from patients suffering from vaginal candidiasis. Each Candida albicans isolate was first cultured in YCB-BSA medium, incubated for 24 h at 35 ºC. Then, 100 µL of triangular gold nanoparticles at three concentrations (16, 32, and 64 µg/mL) were added to Candida suspension, and incubated for 24 and 48 h at 35 ºC. To evaluate Sap activity, 0.1 mL of medium and 0.4 mL of 0.1 M sodium citrate buffer (pH 3.2) containing BSA 1% w/v were added, and incubated 15 minutes at 37 ºC. Then, the optical density of each tube was read at 280 nm. Enzyme activity was expressed as the amount (µM) of tyrosine equivalents released per min per ml of culture supernatant. Results: This study showed that the size of the nanoparticles was 70±50 nm. Sap activity evaluation demonstrated triangular gold nanoparticles could inhibit the enzyme, and the higher incubation time and concentration led to more decrease of Sap activity. Conclusion:For the first time, we demonstrated triangular gold nanoparticles as a novel inhibitor of Sap enzyme which may be useful for treatment of candidiasis.  
topic Candida albicans
Peptide ligand
Secreted aspartyl proteinase
Triangular gold nanoparticles
url http://nmj.mums.ac.ir/pdf_3469_2c9dfb42ef4f6d96540623e1c5a151c4.html
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