Ultrasensitive electrochemical detection of biotin using electrically addressable site-oriented antibody immobilization approach via aminophenyl boronic acid

Ho, Ja‐an Annie; Hsu, Wei Ling; Liao, Wensheng; Chiu, Je Kuan; Chen, Mu Lin; Chang, Heng Chia; Li, Chun Cheng

doi:10.1016/j.bios.2010.08.048

Cited by 89 publications

(36 citation statements)

References 36 publications

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“…The incorporation of a biological recognition element provides specificity for the voltammetric assay. The group reported further developments for a biotin immunosensor [57]; the two complex biosensors (depicted in Figure 7) use different binding techniques to enhance the orientation of antibodies on the SPCE surface. The most sensitive biosensor exploits the affinity of a sugar moiety on the anti-biotin antibody for the boronic acid-modified graphite surface.…”

Section: Screen-printed Carbon Electrodes For Vitamin Analysismentioning

confidence: 99%

Recent Advances in the Fabrication and Application of Screen-Printed Electrochemical (Bio)Sensors Based on Carbon Materials for Biomedical, Agri-Food and Environmental Analyses

et al. 2016

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This review describes recent advances in the fabrication of electrochemical (bio)sensors based on screen-printing technology involving carbon materials and their application in biomedical, agri-food and environmental analyses. It will focus on the various strategies employed in the fabrication of screen-printed (bio)sensors, together with their performance characteristics; the application of these devices for the measurement of selected naturally occurring biomolecules, environmental pollutants and toxins will be discussed.

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Section: Screen-printed Carbon Electrodes For Vitamin Analysismentioning

confidence: 99%

Recent Advances in the Fabrication and Application of Screen-Printed Electrochemical (Bio)Sensors Based on Carbon Materials for Biomedical, Agri-Food and Environmental Analyses

et al. 2016

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“…The currently used techniques are in principle based on these studies and they have been applied to a variety of IgG molecules (Kato et al 1976, Karyakin et al 2000, Cho et al 2007, Pereira and Lai 2008, Cho et al 2009, Billah et al 2010, Ho et al 2010, Hu et al 2010, KausaiteMinkstimiene et al 2010, Wu et al 2014). Another of their advantages is that in cases when the amount of antibody is limited, it enables the reduction and/or conjugation procedures to be tested using other IgG antibodies at first.…”

Section: Introductionmentioning

confidence: 99%

“…One of them is following the established protocol (Hermanson 2008) not taking the antibody type into consideration (Karyakin et al 2000, Billah et al 2010, Ho et al 2010, Hu et al 2010. The second one is tailoring the reduction conditions to particular antibodies resulting in many rather widely distributed adaptations of the original protocol (Kato et al 1976, Cho et al 2007, Pereira and Lai 2008, Kausaite-Minkstimiene et al 2010).…”

Section: Introductionmentioning

confidence: 99%

Considerations in producing preferentially reduced half-antibody fragments

Makaraviciute

Jackson

Millner

et al. 2016

Journal of Immunological Methods

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Half-antibody fragments are a promising reagent for biosensing, drug-delivery and labeling applications, since exposure of the free thiol group in the Fc hinge region allows oriented Preferential reduction of rabbit anti-myoglobin IgG antibodies was optimized and the highest half-antibody yield was obtained with 35 mM TCEP. Finally, it has been demonstrated that produced anti-myoglobin half-IgG fragments retained their binding activity.

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“…The appearance of darker spots in the former method may be because of the increased capture of AuNPs on the slide surface. This increased capture may occur because the surface-conjugated BAs direct the formation of cyclic boronate diesters with the diol groups of glycans at the Fc region of the antibody, thereby leaving the Fab region exposed to the interface for enhanced antigen capture [50] and leading to a greater number of AuNP seeds available for nucleation. The results strongly suggest that the orientation of antibodies on the microarray is significant for the enhancement of the detection sensitivity.…”

Section: Resultsmentioning

confidence: 98%

Fabrication of Highly Stable Glyco‐Gold Nanoparticles and Development of a Glyco‐Gold Nanoparticle‐Based Oriented Immobilized Antibody Microarray for Lectin (GOAL) Assay

Huang

Adak

et al. 2015

Chemistry A European J

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The design of high-affinity lectin ligands is critical for enhancing the inherently weak binding affinities of monomeric carbohydrates to their binding proteins. Glyco-gold nanoparticles (glyco-AuNPs) are promising multivalent glycan displays that can confer significantly improved functional affinity of glyco-AuNPs to proteins. Here, AuNPs are functionalized with several different carbohydrates to profile lectin affinities. We demonstrate that AuNPs functionalized with mixed thiolated ligands comprising glycan (70 mol %) and an amphiphilic linker (30 mol %) provide long-term stability in solutions containing high concentrations of salts and proteins, with no evidence of nonspecific protein adsorption. These highly stable glyco-AuNPs enable the detection of model plant lectins such as Concanavalin A, wheat germ agglutinin, and Ricinus communis Agglutinin 120, at subnanomolar and low picomolar levels through UV/Vis spectrophotometry and dynamic light scattering, respectively. Moreover, we develop in situ glyco-AuNPs-based agglutination on an oriented immobilized antibody microarray, which permits highly sensitive lectin sensing with the naked eye. In addition, this microarray is capable of detecting lectins presented individually, in other environmental settings, or in a mixture of samples. These results indicate that glyconanoparticles represent a versatile and highly sensitive method for detecting and probing the binding of glycan to proteins, with significant implications for the construction of a variety of platforms for the development of glyconanoparticle-based biosensors.

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Ultrasensitive electrochemical detection of biotin using electrically addressable site-oriented antibody immobilization approach via aminophenyl boronic acid

Cited by 89 publications

References 36 publications

Recent Advances in the Fabrication and Application of Screen-Printed Electrochemical (Bio)Sensors Based on Carbon Materials for Biomedical, Agri-Food and Environmental Analyses

Recent Advances in the Fabrication and Application of Screen-Printed Electrochemical (Bio)Sensors Based on Carbon Materials for Biomedical, Agri-Food and Environmental Analyses

Considerations in producing preferentially reduced half-antibody fragments

Fabrication of Highly Stable Glyco‐Gold Nanoparticles and Development of a Glyco‐Gold Nanoparticle‐Based Oriented Immobilized Antibody Microarray for Lectin (GOAL) Assay

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