Visual Detection of Copper(II) by Azide‐ and Alkyne‐Functionalized Gold Nanoparticles Using Click Chemistry

Zhou, Yang; Wang, Shixing; Zhang, Ke; Jiang, Xingyu

doi:10.1002/ange.200802317

Cited by 120 publications

(100 citation statements)

References 55 publications

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“…Various metal ions were detected by monitoring the color changes occurring upon aggregation of ligand-functionalized AuNPs through specific molecular interactions [26][27][28][29][30]. However, studies on colorimetric anion recognition and sensing anions by AuNPs are limited [31][32][33][34][35][36].…”

Section: Introductionmentioning

confidence: 99%

Incorporation of the fluoride induced SiO bond cleavage and functionalized gold nanoparticle aggregation into one colorimetric probe for highly specific and sensitive detection of fluoride

Sun

Zhang

et al. 2014

Analytica Chimica Acta

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Section: Introductionmentioning

confidence: 99%

Incorporation of the fluoride induced SiO bond cleavage and functionalized gold nanoparticle aggregation into one colorimetric probe for highly specific and sensitive detection of fluoride

Sun

Zhang

et al. 2014

Analytica Chimica Acta

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“…[55] The enzyme on the secondary antibody are replaced by copper monoxide nanoparticle (CuO NP). After finishing the immunoreaction, the Cu 2+ was released into the solution by hydrochloric acids, which then was reduced by the added sodium ascorbate to mediate the CuAAC click reaction between azide-and alkyne-modified AuNPs.…”

Section: Materials For Enhanced Immunoassaymentioning

confidence: 99%

Materials for Microfluidic Immunoassays: A Review

Mou

Jiang

2017

Adv Healthcare Materials

Self Cite

118

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Conventional immunoassays suffer from at least one of these following limitations: long processing time, high costs, poor user‐friendliness, technical complexity, poor sensitivity and specificity. Microfluidics, a technology characterized by the engineered manipulation of fluids in channels with characteristic lengthscale of tens of micrometers, has shown considerable promise for improving immunoassays that could overcome these limitations in medical diagnostics and biology research. The combination of microfluidics and immunoassay can detect biomarkers with faster assay time, reduced volumes of reagents, lower power requirements, and higher levels of integration and automation compared to traditional approaches. This review focuses on the materials‐related aspects of the recent advances in microfluidics‐based immunoassays for point‐of‐care (POC) diagnostics of biomarkers. We compare the materials for microfluidic chips fabrication in five aspects: fabrication, integration, function, modification and cost, and describe their advantages and drawbacks. In addition, we review materials for modifying antibodies to improve the performance of the reaction of immunoassay. We also review the state of the art in microfluidic immunoassays POC platforms, from the laboratory to routine clinical practice, and also commercial products in the market. Finally, we discuss the current challenges and future developments in microfluidic immunoassays.

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“…Thermal denaturation of MOF proteins was measured in the buffer containing 25 mM Na-HEPES, pH 7.0, 100 mM NaCl, 1 mM EDTA, 5% glycerol, The solid 3-bromopropionic acid (7.65 g, 50 mmol) and sodium azide (6.5 g, 100 mmol) were dissolved in 20 mL anhydrous DMF and stirred in a 50 mL round-bottom flask (Scheme 3.4), the mixture was refluxed for 4 h after which solution was concentrated by removing DMF. 142 Ethyl acetate (800 mL) was added into the flask and the solution was extracted with 0.1 M HCl (2×30 mL), ddH 2 O (30 mL) and brine (30 mL). The organic layer was dried with anhydrous MgSO 4 , filtered, and evaporated.…”

Section: Thermal Denaturation Assay Of Mof Proteinmentioning

confidence: 99%

Histone Acetyltransferases

2005

Encyclopedic Reference of Genomics and Proteomics in Molecular Medicine

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As an important posttranslational modification, protein acetylation plays critical roles in many biological processes such as gene transcription, DNA damage repair, apoptosis and metabolism. The acetylation occurs on the ε-amino group of specific lysine residues, and is catalyzed by histone acetyltransferases (HATs). In cellular contexts, HATs are found to target hundreds and thousands of substrates including histone and nonhistone proteins. Lysine acetylation changes the microenvironment of protein and may potentially alter protein activity and protein-protein interaction. The goal of this dissertation project is to investigate the impact of lysine acetylation on the catalysis of MYST HATs, and to establish the strategy for labeling substrates of the MYST HATs at cellular level. To understand the regulatory mechanism of MYST HATs, a detailed study was carried out to investigate the active site lysine acetylation of two MYST HATs (MOF and Tip60). Autoradiography and immunoblotting data shows that mutation of active site lysine differentially affects the enzyme autoacetylation activity and the cognate substrate acetylation activity. In addition, deacetylated MOF and Tip60 were prepared by using the nonspecific lysine deacetylase Sirt1. Kinetic study demonstrated that the acetylation of the active site lysine on MYST HATs marginally modulates the HAT catalysis. This work provides new insights into the regulatory mechanism of MYST catalysis. In the second part of my work, we designed and synthesized a series of Ac-CoA analogs conjugated with alkynyl or azido functional groups. Meanwhile, the active site of the MOF was engineered to expand the cofactor binding capability. Fluorescence screening was carried out to characterize the enzyme activity to Ac-CoA analogs. MOF-I317A with all analogs and MOF-I317A/H273A-5HYCoA were identified and further applied in the labeling of the cognate histone H4 protein and HAT substrates in 293T cell lysate. Visualizing of the labeled substrate was achieved using the alkynyl or azido-tagged fluorescent reporters through the copper-catalyzed azide−alkyne cycloaddi on.As expected, the histone H4 protein was successfully labeled by the active enzyme-cofactor pairs. More intriguingly, multiple protein bands in cell lysate were labeled and observed. This work provides a new versatile strategy in exploring the substrates of MYST HATs at the proteomic level.

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Visual Detection of Copper(II) by Azide‐ and Alkyne‐Functionalized Gold Nanoparticles Using Click Chemistry

Cited by 120 publications

References 55 publications

Incorporation of the fluoride induced SiO bond cleavage and functionalized gold nanoparticle aggregation into one colorimetric probe for highly specific and sensitive detection of fluoride

Incorporation of the fluoride induced SiO bond cleavage and functionalized gold nanoparticle aggregation into one colorimetric probe for highly specific and sensitive detection of fluoride

Materials for Microfluidic Immunoassays: A Review

Histone Acetyltransferases

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