Nanostructured electrochemical biosensor for th0065 detection of the weak binding between the dengue virus and the CLEC5A receptor

In this paper, we develop an effective method for detecting weak molecular bonding between the dengue virus (DV) and its receptor C-type lectin domain family 5, member A (CLEC5A). The CLEC5A–DV interaction is critical for DV-induced hemorrhagic fever and shock syndrome, so the sensing of CLEC5A–DV b...

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Published inNanomedicine Vol. 10; no. 6; pp. 1335 - 1341
Main Authors Tung, Yen-Ting, Wu, Ming-Fang, Wang, Gou-Jen, Hsieh, Shie-Liang
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.08.2014
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Abstract In this paper, we develop an effective method for detecting weak molecular bonding between the dengue virus (DV) and its receptor C-type lectin domain family 5, member A (CLEC5A). The CLEC5A–DV interaction is critical for DV-induced hemorrhagic fever and shock syndrome, so the sensing of CLEC5A–DV binding is crucial to realize a thorough study of the pathogenesis of dengue fever. Through a highly sensitive nanostructured sensing electrode of gold nanoparticles (GNPs) uniformly deposited on a nanohemisphere array, a label-free detection of the ultra weak binding between CLEC5A and the DV can be performed with electrochemical impedance spectroscopy (EIS). Experimental results demonstrate that the proposed approach is a highly promising method for investigating weak molecular interactions such as the ligand–receptor interaction of dengue fever, enterovirus (EV), or the interaction between cancer surface glycoproteins and their receptors. Authors of this study investigated the ultra-weak binding between dengue virus and its CLEC5A receptor via electrochemical impedance spectroscopy and gold NP sensing electrode. Similar methods may be applicable in other infections and in cancer models as well. An effective method for detecting weak molecular bonding between the dengue virus (DV) and its receptor C-type lectin domain family 5, member A (CLEC5A) has been developed. Label-free detections of the ultra weak binding were carried out via a highly sensitive nanostructured sensing electrode with gold nanoparticles (GNPs) uniformly deposited on a nanohemisphere array. Experimental results demonstrate that the proposed approach is a highly promising method for investigating weak molecular interactions such as the ligand–receptor interaction of DV and enterovirus. [Display omitted]
AbstractList Abstract In this paper, we develop an effective method for detecting weak molecular bonding between the dengue virus (DV) and its receptor C-type lectin domain family 5, member A (CLEC5A). The CLEC5A–DV interaction is critical for DV-induced hemorrhagic fever and shock syndrome, so the sensing of CLEC5A–DV binding is crucial to realize a thorough study of the pathogenesis of dengue fever. Through a highly sensitive nanostructured sensing electrode of gold nanoparticles (GNPs) uniformly deposited on a nanohemisphere array, a label-free detection of the ultra weak binding between CLEC5A and the DV can be performed with electrochemical impedance spectroscopy (EIS). Experimental results demonstrate that the proposed approach is a highly promising method for investigating weak molecular interactions such as the ligand–receptor interaction of dengue fever, enterovirus (EV), or the interaction between cancer surface glycoproteins and their receptors. From the Clinical Editor Authors of this study investigated the ultra-weak binding between dengue virus and its CLEC5A receptor via electrochemical impedance spectroscopy and gold NP sensing electrode. Similar methods may be applicable in other infections and in cancer models as well.
In this paper, we develop an effective method for detecting weak molecular bonding between the dengue virus (DV) and its receptor C-type lectin domain family 5, member A (CLEC5A). The CLEC5A-DV interaction is critical for DV-induced hemorrhagic fever and shock syndrome, so the sensing of CLEC5A-DV binding is crucial to realize a thorough study of the pathogenesis of dengue fever. Through a highly sensitive nanostructured sensing electrode of gold nanoparticles (GNPs) uniformly deposited on a nanohemisphere array, a label-free detection of the ultra weak binding between CLEC5A and the DV can be performed with electrochemical impedance spectroscopy (EIS). Experimental results demonstrate that the proposed approach is a highly promising method for investigating weak molecular interactions such as the ligand-receptor interaction of dengue fever, enterovirus (EV), or the interaction between cancer surface glycoproteins and their receptors. Authors of this study investigated the ultra-weak binding between dengue virus and its CLEC5A receptor via electrochemical impedance spectroscopy and gold NP sensing electrode. Similar methods may be applicable in other infections and in cancer models as well.
In this paper, we develop an effective method for detecting weak molecular bonding between the dengue virus (DV) and its receptor C-type lectin domain family 5, member A (CLEC5A). The CLEC5A-DV interaction is critical for DV-induced hemorrhagic fever and shock syndrome, so the sensing of CLEC5A-DV binding is crucial to realize a thorough study of the pathogenesis of dengue fever. Through a highly sensitive nanostructured sensing electrode of gold nanoparticles (GNPs) uniformly deposited on a nanohemisphere array, a label-free detection of the ultra weak binding between CLEC5A and the DV can be performed with electrochemical impedance spectroscopy (EIS). Experimental results demonstrate that the proposed approach is a highly promising method for investigating weak molecular interactions such as the ligand-receptor interaction of dengue fever, enterovirus (EV), or the interaction between cancer surface glycoproteins and their receptors.In this paper, we develop an effective method for detecting weak molecular bonding between the dengue virus (DV) and its receptor C-type lectin domain family 5, member A (CLEC5A). The CLEC5A-DV interaction is critical for DV-induced hemorrhagic fever and shock syndrome, so the sensing of CLEC5A-DV binding is crucial to realize a thorough study of the pathogenesis of dengue fever. Through a highly sensitive nanostructured sensing electrode of gold nanoparticles (GNPs) uniformly deposited on a nanohemisphere array, a label-free detection of the ultra weak binding between CLEC5A and the DV can be performed with electrochemical impedance spectroscopy (EIS). Experimental results demonstrate that the proposed approach is a highly promising method for investigating weak molecular interactions such as the ligand-receptor interaction of dengue fever, enterovirus (EV), or the interaction between cancer surface glycoproteins and their receptors.Authors of this study investigated the ultra-weak binding between dengue virus and its CLEC5A receptor via electrochemical impedance spectroscopy and gold NP sensing electrode. Similar methods may be applicable in other infections and in cancer models as well.FROM THE CLINICAL EDITORAuthors of this study investigated the ultra-weak binding between dengue virus and its CLEC5A receptor via electrochemical impedance spectroscopy and gold NP sensing electrode. Similar methods may be applicable in other infections and in cancer models as well.
In this paper, we develop an effective method for detecting weak molecular bonding between the dengue virus (DV) and its receptor C-type lectin domain family 5, member A (CLEC5A). The CLEC5A–DV interaction is critical for DV-induced hemorrhagic fever and shock syndrome, so the sensing of CLEC5A–DV binding is crucial to realize a thorough study of the pathogenesis of dengue fever. Through a highly sensitive nanostructured sensing electrode of gold nanoparticles (GNPs) uniformly deposited on a nanohemisphere array, a label-free detection of the ultra weak binding between CLEC5A and the DV can be performed with electrochemical impedance spectroscopy (EIS). Experimental results demonstrate that the proposed approach is a highly promising method for investigating weak molecular interactions such as the ligand–receptor interaction of dengue fever, enterovirus (EV), or the interaction between cancer surface glycoproteins and their receptors. Authors of this study investigated the ultra-weak binding between dengue virus and its CLEC5A receptor via electrochemical impedance spectroscopy and gold NP sensing electrode. Similar methods may be applicable in other infections and in cancer models as well. An effective method for detecting weak molecular bonding between the dengue virus (DV) and its receptor C-type lectin domain family 5, member A (CLEC5A) has been developed. Label-free detections of the ultra weak binding were carried out via a highly sensitive nanostructured sensing electrode with gold nanoparticles (GNPs) uniformly deposited on a nanohemisphere array. Experimental results demonstrate that the proposed approach is a highly promising method for investigating weak molecular interactions such as the ligand–receptor interaction of DV and enterovirus. [Display omitted]
Author Wu, Ming-Fang
Hsieh, Shie-Liang
Tung, Yen-Ting
Wang, Gou-Jen
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Issue 6
Keywords Anodic aluminum oxide
Nanostructured biosensor
Dengue virus
CLEC5A
Electrochemical impedance spectroscopy
Language English
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Snippet In this paper, we develop an effective method for detecting weak molecular bonding between the dengue virus (DV) and its receptor C-type lectin domain family...
Abstract In this paper, we develop an effective method for detecting weak molecular bonding between the dengue virus (DV) and its receptor C-type lectin domain...
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SubjectTerms Anodic aluminum oxide
Biosensing Techniques - instrumentation
CLEC5A
Dengue - metabolism
Dengue virus
Dengue Virus - metabolism
Dielectric Spectroscopy - instrumentation
Electrochemical impedance spectroscopy
Electrodes
Equipment Design
Gold - chemistry
Humans
Internal Medicine
Lectins, C-Type - metabolism
Nanostructured biosensor
Nanostructures - chemistry
Nanostructures - ultrastructure
Protein Binding
Receptors, Cell Surface - metabolism
Title Nanostructured electrochemical biosensor for th0065 detection of the weak binding between the dengue virus and the CLEC5A receptor
URI https://www.clinicalkey.com/#!/content/1-s2.0-S1549963414001270
https://www.clinicalkey.es/playcontent/1-s2.0-S1549963414001270
https://dx.doi.org/10.1016/j.nano.2014.03.009
https://www.ncbi.nlm.nih.gov/pubmed/24674971
https://www.proquest.com/docview/1551331356
Volume 10
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