Protein immobilization on carbon nanotubes via a two-step process of diimide-activated amidation

Jiang, Kuiyang; Schadler, Linda S.; Siegel, Richard W.; Zhang, Xinjie; Zhang, Haifeng; Terrones, Mauricio

doi:10.1039/b310359e

Cited by 362 publications

(240 citation statements)

References 18 publications

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“…On the other hand, covalent conjugation provides durable attachment, but the harsh oxidation step (e.g., with strong acids) disrupts the π-networks on the CNT surfaces and may diminish their mechanical and electronic properties (11). Covalent attachment of proteins on carboxylated CNTs using the popular cross-linker 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) was first reported by Huang et al (12) and Jiang et al (13). Since then, it has been widely used in the covalent immobilization of proteins on carboxylated CNTs in biosensing studies (14)(15)(16)(17)(18)(19)(20)(21)(22).…”

Section: Introductionmentioning

confidence: 99%

Covalent Immobilization of Proteins on Carbon Nanotubes Using the Cross-Linker 1-Ethyl-3-(3-dimethylaminopropyl)carbodiimide—a Critical Assessment

2008

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Functionalization of carbon nanotubes (CNTs) with proteins is often a key step in their biological applications, particularly in biosensing. One popular method has used the cross-linker 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) to covalently conjugate proteins onto carboxylated CNTs. In this article, we critically assess the evidence presented in these conjugation studies in the literature. As CNTs have a natural affinity for diverse proteins through hydrophobic and electrostatic interactions, it is therefore important to differentiate protein covalent attachment from adsorption in the immobilization mechanism. Unfortunately, many studies of conjugating proteins onto CNTs using EDC lacked essential controls to eliminate the possibility of protein adsorption. In studies where the attachment was claimed to be covalent, discrepancies existed and the observed immobilization appeared to be due to adsorption. So far, bond analysis has been lacking to ascertain the nature of the attachment using EDC. We recommend that this approach of covalent immobilization of proteins on CNTs be re-evaluated and treated with caution.

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Section: Introductionmentioning

confidence: 99%

Covalent Immobilization of Proteins on Carbon Nanotubes Using the Cross-Linker 1-Ethyl-3-(3-dimethylaminopropyl)carbodiimide—a Critical Assessment

2008

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“…Using this concept, various carbon nanotube systems could be designed using specific biotinylated antibodies corresponding to the targeted proteins. 16 The streptavidin-biotin complex shows the highestaffinity noncovalent interaction (binding constant, 10 -15 M).…”

Section: Discussionmentioning

confidence: 99%

Preparation and binding study of a complex made of DNA-treated single-walled carbon nanotubes and antibody for specific delivery of a “molecular heater” platform

Kawaguchi

Yamazaki²,

Ohno³

et al. 2012

IJN

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Abstract:Carbon nanotubes have been explored as heat-delivery vehicles for thermal ablation of tumors. To use single-walled carbon nanotubes (SWNT) as a "molecular heater" for hyperthermia therapy in cancer, stable dispersibility and smart-delivery potential will be needed, as well as lack of toxicity. This paper reports the preparation of a model complex comprising DNA-treated SWNT and anti-human IgG antibody and the specific binding ability of this model complex with the targeted protein, ie, human IgG. Treatment with double-stranded DNA enabled stable dispersibility of a complex composed of SWNT and the antibody under physiological conditions. Quartz crystal microbalance results suggest that there was one immobilized IgG molecule to every 21,700 carbon atoms in the complex containing DNA-treated SWNT and the antibody. The DNA-SWNT antibody complex showed good selectivity for binding to the targeted protein. Binding analysis revealed that treatment with DNA did not interfere with binding affinity or capacity between the immobilized antibody and the targeted protein. The results of this study demonstrate that the DNA-SWNT antibody complex is a useful tool for use as a smart "molecular heater" platform applicable to various types of antibodies targeting a specific antigen.

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“…This was done by the well know EDAC/NHS chemistry, where the À COOH group forms a highly reactive O-acylisourea intermediate that reacts rapidly with NHS to produce a more stable succinimydyl ester intermediate (Jiang et al, 2004). The resulting ester undertakes easy nucleophilic substitution with the amine groups on the Au/amine layer.…”

Section: Immunosensor Designmentioning

confidence: 99%

Disposable immunosensor using a simple method for oriented antibody immobilization for label-free real-time detection of an oxidative stress biomarker implicated in cancer diseases

Ferreira

Sales

2014

Biosensors and Bioelectronics

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a b s t r a c tThis work proposes a novel approach for a suitable orientation of antibodies (Ab) on an immunosensing platform, applied here to the determination of 8-hydroxy-2′-deoxyguanosine (8OHdG), a biomarker of oxidative stress that has been associated to chronic diseases, such as cancer. The anti-8OHdG was bound to an amine modified gold support through its Fc region after activation of its carboxylic functions. Nonoriented approaches of Ab binding to the platform were tested in parallel, in order to show that the presented methodology favored Ab/Ag affinity and immunodetection of the antigen.The immunosensor design was evaluated by quartz-crystal microbalance with dissipation, atomic force microscopy, electrochemical impedance spectroscopy (EIS) and square-wave voltammetry. EIS was also a suitable technique to follow the analytical behavior of the device against 8OHdG. The affinity binding between 8OHdG and the antibody immobilized in the gold modified platform increased the charge transfer resistance across the electrochemical set-up. The observed behavior was linear from 0.02 to 7.0 ng/mL of 8OHdG concentrations. The interference from glucose, urea and creatinine was found negligible. An attempt of application to synthetic samples was also successfully conducted.Overall, the presented approach enabled the production of suitably oriented Abs over a gold platform by means of a much simpler process than other oriented-Ab binding approaches described in the literature, as far as we know, and was successful in terms of analytical features and sample application.

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Protein immobilization on carbon nanotubes via a two-step process of diimide-activated amidation

Cited by 362 publications

References 18 publications

Covalent Immobilization of Proteins on Carbon Nanotubes Using the Cross-Linker 1-Ethyl-3-(3-dimethylaminopropyl)carbodiimide—a Critical Assessment

Covalent Immobilization of Proteins on Carbon Nanotubes Using the Cross-Linker 1-Ethyl-3-(3-dimethylaminopropyl)carbodiimide—a Critical Assessment

Preparation and binding study of a complex made of DNA-treated single-walled carbon nanotubes and antibody for specific delivery of a “molecular heater” platform

Disposable immunosensor using a simple method for oriented antibody immobilization for label-free real-time detection of an oxidative stress biomarker implicated in cancer diseases

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Protein immobilization on carbon nanotubes via a two-step process of diimide-activated amidation

Cited by 362 publications

References 18 publications

Covalent Immobilization of Proteins on Carbon Nanotubes Using the Cross-Linker 1-Ethyl-3-(3-dimethylaminopropyl)carbodiimide—a Critical Assessment

Covalent Immobilization of Proteins on Carbon Nanotubes Using the Cross-Linker 1-Ethyl-3-(3-dimethylaminopropyl)carbodiimide—a Critical Assessment

Preparation and binding study of a complex made of DNA-treated single-walled carbon nanotubes and antibody for specific delivery of a &ldquo;molecular heater&rdquo; platform

Disposable immunosensor using a simple method for oriented antibody immobilization for label-free real-time detection of an oxidative stress biomarker implicated in cancer diseases

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Preparation and binding study of a complex made of DNA-treated single-walled carbon nanotubes and antibody for specific delivery of a “molecular heater” platform