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Peptide-Templated Gold Clusters as Enzyme-Like Catalyst Boost Intracellular Oxidative Pressure and Induce Tumor-Specific Cell Apoptosis
Anticancer metallodrugs that aim to physiological characters unique to tumor microenvironment are expected to combat drug tolerance and side-effects. Recently, owing to the fact that reactive oxygen species’ is closely related to the development of tumors, people are committed to developing metallod...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6316732/ https://www.ncbi.nlm.nih.gov/pubmed/30545158 http://dx.doi.org/10.3390/nano8121040 |
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author | Zhang, Ya Zhang, Xiangchun Yuan, Qing Niu, Wenchao Zhang, Chunyu Li, Jiaojiao He, Zhesheng Tang, Yuhua Ren, Xiaojun Zhang, Zhichao Cai, Pengju Gao, Liang Gao, Xueyun |
author_facet | Zhang, Ya Zhang, Xiangchun Yuan, Qing Niu, Wenchao Zhang, Chunyu Li, Jiaojiao He, Zhesheng Tang, Yuhua Ren, Xiaojun Zhang, Zhichao Cai, Pengju Gao, Liang Gao, Xueyun |
author_sort | Zhang, Ya |
collection | PubMed |
description | Anticancer metallodrugs that aim to physiological characters unique to tumor microenvironment are expected to combat drug tolerance and side-effects. Recently, owing to the fact that reactive oxygen species’ is closely related to the development of tumors, people are committed to developing metallodrugs with the capacity of improving the level of reactive oxygen species level toinduce oxidative stress in cancer cells. Herein, we demonstrated that peptide templated gold clusters with atomic precision preferably catalyze the transformation of hydrogen peroxide into superoxide anion in oxidative pressure-type tumor cells. Firstly, we successfully constructed gold clusters by rationally designing peptide sequences which targets integrin α(ν)β(3) overexpressed on glioblastoma cells. The superoxide anion, radical derived from hydrogen peroxide and catalyzed by gold clusters, was confirmed in vitro under pseudo-physiological conditions. Then, kinetic parameters were evaluated to verify the catalytic properties of gold clusters. Furthermore, these peptide decorated clusters can serve as special enzyme-like catalyst to convert endogenous hydrogen peroxide into superoxide anion, elevated intracellular reactive oxygen species levels, lower mitochondrial membrane potential, damage biomacromolecules, and trigger tumor cell apoptosis consequently. |
format | Online Article Text |
id | pubmed-6316732 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-63167322019-01-10 Peptide-Templated Gold Clusters as Enzyme-Like Catalyst Boost Intracellular Oxidative Pressure and Induce Tumor-Specific Cell Apoptosis Zhang, Ya Zhang, Xiangchun Yuan, Qing Niu, Wenchao Zhang, Chunyu Li, Jiaojiao He, Zhesheng Tang, Yuhua Ren, Xiaojun Zhang, Zhichao Cai, Pengju Gao, Liang Gao, Xueyun Nanomaterials (Basel) Article Anticancer metallodrugs that aim to physiological characters unique to tumor microenvironment are expected to combat drug tolerance and side-effects. Recently, owing to the fact that reactive oxygen species’ is closely related to the development of tumors, people are committed to developing metallodrugs with the capacity of improving the level of reactive oxygen species level toinduce oxidative stress in cancer cells. Herein, we demonstrated that peptide templated gold clusters with atomic precision preferably catalyze the transformation of hydrogen peroxide into superoxide anion in oxidative pressure-type tumor cells. Firstly, we successfully constructed gold clusters by rationally designing peptide sequences which targets integrin α(ν)β(3) overexpressed on glioblastoma cells. The superoxide anion, radical derived from hydrogen peroxide and catalyzed by gold clusters, was confirmed in vitro under pseudo-physiological conditions. Then, kinetic parameters were evaluated to verify the catalytic properties of gold clusters. Furthermore, these peptide decorated clusters can serve as special enzyme-like catalyst to convert endogenous hydrogen peroxide into superoxide anion, elevated intracellular reactive oxygen species levels, lower mitochondrial membrane potential, damage biomacromolecules, and trigger tumor cell apoptosis consequently. MDPI 2018-12-12 /pmc/articles/PMC6316732/ /pubmed/30545158 http://dx.doi.org/10.3390/nano8121040 Text en © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Zhang, Ya Zhang, Xiangchun Yuan, Qing Niu, Wenchao Zhang, Chunyu Li, Jiaojiao He, Zhesheng Tang, Yuhua Ren, Xiaojun Zhang, Zhichao Cai, Pengju Gao, Liang Gao, Xueyun Peptide-Templated Gold Clusters as Enzyme-Like Catalyst Boost Intracellular Oxidative Pressure and Induce Tumor-Specific Cell Apoptosis |
title | Peptide-Templated Gold Clusters as Enzyme-Like Catalyst Boost Intracellular Oxidative Pressure and Induce Tumor-Specific Cell Apoptosis |
title_full | Peptide-Templated Gold Clusters as Enzyme-Like Catalyst Boost Intracellular Oxidative Pressure and Induce Tumor-Specific Cell Apoptosis |
title_fullStr | Peptide-Templated Gold Clusters as Enzyme-Like Catalyst Boost Intracellular Oxidative Pressure and Induce Tumor-Specific Cell Apoptosis |
title_full_unstemmed | Peptide-Templated Gold Clusters as Enzyme-Like Catalyst Boost Intracellular Oxidative Pressure and Induce Tumor-Specific Cell Apoptosis |
title_short | Peptide-Templated Gold Clusters as Enzyme-Like Catalyst Boost Intracellular Oxidative Pressure and Induce Tumor-Specific Cell Apoptosis |
title_sort | peptide-templated gold clusters as enzyme-like catalyst boost intracellular oxidative pressure and induce tumor-specific cell apoptosis |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6316732/ https://www.ncbi.nlm.nih.gov/pubmed/30545158 http://dx.doi.org/10.3390/nano8121040 |
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