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The Antibacterial Assay of Tectorigenin with Detergents or ATPase Inhibitors against Methicillin-Resistant Staphylococcus aureus
Tectorigenin (TTR) is an O-methylated isoflavone derived from the rhizome of Belamacanda chinensis (L.) DC. It is known to perform a wide spectrum of biological activities such as antioxidant, anti-inflammatory, anti-tumor. The aim of this study is to examine the mechanism of antibacterial activity...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4058531/ https://www.ncbi.nlm.nih.gov/pubmed/24987433 http://dx.doi.org/10.1155/2014/716509 |
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author | Joung, Dae-Ki Mun, Su-Hyun Lee, Kuang-Shim Kang, Ok-Hwa Choi, Jang-Gi Kim, Sung-Bae Gong, Ryong Chong, Myong-Soo Kim, Youn-Chul Lee, Dong-Sung Shin, Dong-Won Kwon, Dong-Yeul |
author_facet | Joung, Dae-Ki Mun, Su-Hyun Lee, Kuang-Shim Kang, Ok-Hwa Choi, Jang-Gi Kim, Sung-Bae Gong, Ryong Chong, Myong-Soo Kim, Youn-Chul Lee, Dong-Sung Shin, Dong-Won Kwon, Dong-Yeul |
author_sort | Joung, Dae-Ki |
collection | PubMed |
description | Tectorigenin (TTR) is an O-methylated isoflavone derived from the rhizome of Belamacanda chinensis (L.) DC. It is known to perform a wide spectrum of biological activities such as antioxidant, anti-inflammatory, anti-tumor. The aim of this study is to examine the mechanism of antibacterial activity of TTR against methicillin-resistant Staphylococcus aureus (MRSA). The anti-MRSA activity of TTR was analyzed in combination assays with detergent, ATPase inhibitors, and peptidoglycan (PGN) derived from S. aureus. Transmission electron microscopy (TEM) was used to monitor survival characteristics and changes in S. aureus morphology. The MIC values of TTR against all the tested strains were 125 μg/mL. The OD(600) of each suspension treated with a combination of Triton X-100, DCCD, and NaN(3) with TTR (1/10 × MIC) had been reduced from 68% to 80%, compared to the TTR alone. At a concentration of 125 μg/mL, PGN blocked antibacterial activity of TTR. This study indicates that anti-MRSA action of TTR is closely related to cytoplasmic membrane permeability and ABC transporter, and PGN at 125 μg/mL directly bind to and inhibit TTR at 62.5 μg/mL. These results can be important indication in study on antimicrobial activity mechanism against multidrug resistant strains. |
format | Online Article Text |
id | pubmed-4058531 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-40585312014-07-01 The Antibacterial Assay of Tectorigenin with Detergents or ATPase Inhibitors against Methicillin-Resistant Staphylococcus aureus Joung, Dae-Ki Mun, Su-Hyun Lee, Kuang-Shim Kang, Ok-Hwa Choi, Jang-Gi Kim, Sung-Bae Gong, Ryong Chong, Myong-Soo Kim, Youn-Chul Lee, Dong-Sung Shin, Dong-Won Kwon, Dong-Yeul Evid Based Complement Alternat Med Research Article Tectorigenin (TTR) is an O-methylated isoflavone derived from the rhizome of Belamacanda chinensis (L.) DC. It is known to perform a wide spectrum of biological activities such as antioxidant, anti-inflammatory, anti-tumor. The aim of this study is to examine the mechanism of antibacterial activity of TTR against methicillin-resistant Staphylococcus aureus (MRSA). The anti-MRSA activity of TTR was analyzed in combination assays with detergent, ATPase inhibitors, and peptidoglycan (PGN) derived from S. aureus. Transmission electron microscopy (TEM) was used to monitor survival characteristics and changes in S. aureus morphology. The MIC values of TTR against all the tested strains were 125 μg/mL. The OD(600) of each suspension treated with a combination of Triton X-100, DCCD, and NaN(3) with TTR (1/10 × MIC) had been reduced from 68% to 80%, compared to the TTR alone. At a concentration of 125 μg/mL, PGN blocked antibacterial activity of TTR. This study indicates that anti-MRSA action of TTR is closely related to cytoplasmic membrane permeability and ABC transporter, and PGN at 125 μg/mL directly bind to and inhibit TTR at 62.5 μg/mL. These results can be important indication in study on antimicrobial activity mechanism against multidrug resistant strains. Hindawi Publishing Corporation 2014 2014-05-28 /pmc/articles/PMC4058531/ /pubmed/24987433 http://dx.doi.org/10.1155/2014/716509 Text en Copyright © 2014 Dae-Ki Joung et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Joung, Dae-Ki Mun, Su-Hyun Lee, Kuang-Shim Kang, Ok-Hwa Choi, Jang-Gi Kim, Sung-Bae Gong, Ryong Chong, Myong-Soo Kim, Youn-Chul Lee, Dong-Sung Shin, Dong-Won Kwon, Dong-Yeul The Antibacterial Assay of Tectorigenin with Detergents or ATPase Inhibitors against Methicillin-Resistant Staphylococcus aureus |
title | The Antibacterial Assay of Tectorigenin with Detergents or ATPase Inhibitors against Methicillin-Resistant Staphylococcus aureus
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title_full | The Antibacterial Assay of Tectorigenin with Detergents or ATPase Inhibitors against Methicillin-Resistant Staphylococcus aureus
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title_fullStr | The Antibacterial Assay of Tectorigenin with Detergents or ATPase Inhibitors against Methicillin-Resistant Staphylococcus aureus
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title_full_unstemmed | The Antibacterial Assay of Tectorigenin with Detergents or ATPase Inhibitors against Methicillin-Resistant Staphylococcus aureus
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title_short | The Antibacterial Assay of Tectorigenin with Detergents or ATPase Inhibitors against Methicillin-Resistant Staphylococcus aureus
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title_sort | antibacterial assay of tectorigenin with detergents or atpase inhibitors against methicillin-resistant staphylococcus aureus |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4058531/ https://www.ncbi.nlm.nih.gov/pubmed/24987433 http://dx.doi.org/10.1155/2014/716509 |
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