Study of antibody/antigen binding kinetics by total internal reflection ellipsometry

Baleviciute, Ieva; Balevičius, Zigmas; Makaraviciute, Asta; Ramanavičienė, Almira

doi:10.1016/j.bios.2012.07.017

Cited by 58 publications

(27 citation statements)

References 22 publications

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“…As such, the incorporation of antibodies as recognition elements is expected to increase assay sensitivity to subnanomolar level. 10 However, antibody-based strategies often require a sandwich system for screening target proteins. Thus, to identify one target protein, two different antibodies are required, making antibody-based systems impractical for large-scale biomarker discovery.…”

Section: Introductionmentioning

confidence: 99%

Cancer biomarker discovery using DNA aptamers

Cheng

Qiu

et al. 2016

Analyst

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Biomarkers are signature molecules able to indicate specific physiological states of cells. Identification of reliable biomarkers is essential for early diagnosis and adaptive treatment of diseases, especially cancer. Aptamers are single-stranded oligonucleotides generated by an in vitro screening method called Systematic Evolution of Ligands by Exponential Enrichment (SELEX). They can recognize their cognate targets with selectivity and affinity comparable to that of protein antibodies. In addition, aptamers have superiorities including easy synthesis, high chemical stability, convenient modification and flexible design. As such, these DNA molecules show great promise as powerful molecular probes for biomarker discovery and biomarker-based clinical applications. Using complex samples as targets, a panel of aptamers can be systematically generated for comprehensive recognition of disease-specific proteins, which can potentially serve as biomarkers. This review describes current methods for biomarker discovery using aptamers.

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Section: Introductionmentioning

confidence: 99%

Cancer biomarker discovery using DNA aptamers

Cheng

Qiu

et al. 2016

Analyst

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“…A number of techniques exist for the measurement of the antibody-antigen binding kinetics, such as surface plasmon resonance (SPR) spectroscopy, fluorescence polarization, quartz crystal microbalance (QCM) sensing, interferometry and total internal reflection ellipsometry [28,29].…”

Section: Antibody-antigen Binding Kineticsmentioning

confidence: 99%

Indirect competitive enzyme-linked immunosorbent assay of tris-(2,3-dibromopropyl) isocyanurate with monoclonal antibody

Feng

et al. 2014

Talanta

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“…For the same protein layer, the grayscale value is nearly proportional to the mass surface concentration of the protein layer within the range of 0-10 nm [41]. Compared with the SPR technique, TIRIE not only acquires the light intensity information like SPR response, but also provides the ellipsometric phase sensitive results, leading to achieve higher sensitivity [43,44]. 0.1 mg/mL IgG and anti-IgG solutions in PBST and BB were injected in situ, during the experiment.…”

Section: Total Internal Reflection Imaging Ellipsometrymentioning

confidence: 99%

“…Its working principle, as explained in detail in the experimental section, is based on the specific interaction of target molecules with ligands on the surface (nonspecific adsorption must be avoided), which results in an increase of the surface density, quantitatively measured by density changes in grayscale values collected on a CCD camera. Thus, the grayscale reflects the dynamics of the biomolecular interactions over the time, similarly to SPR, but with higher sensitivity [43,44,56].…”

Section: Evaluation Of the Immunosensor Performancementioning

confidence: 99%

Nanostructured interfaces with site-specific bioreceptors for immunosensing

Paiva

Almeida

Marquês

et al. 2017

Applied Surface Science

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a b s t r a c tIn this work, we propose a simple and effective approach to build nanostructured immunosensor platforms. The one-step strategy relies on i) the in situ formation of dithiocarbamates from the reaction between carbon disulfide and amine groups, present on protein A, ii) their attachment to gold nanoparticles (AuNPs), and iii) the linkage of the modified AuNPs to the electrode surface, which depends on the strong interaction between gold substrates and sulfur moieties. AuNPs and protein A are used to increase the surface coverage of Immunoglobulin G (IgG) and promote the oriented immobilization of the antibodies on the immunosensing interface. The modified gold surfaces with biomolecules were thoroughly characterized by a combination of techniques: UV-vis spectrophotometry, conventional ellipsometry and atomic force microscopy. The immunosensor performance was assessed in real-time, by surface plasmon resonance and by the highly sensitive total internal reflection imaging ellipsometry, through the specific biorecognition between anti-IgG and the immobilized IgG molecules. We demonstrate that the presence of AuNPs improves the sensitivity of the anti-IgG specific detection, whereas the presence of co-adsorbed CS 2 is responsible for blocking the undesired protein nonspecific adsorption to the gold substrate. Overall, we report a simple and innovative one-step method, to chemically modify gold surfaces with protein A and AuNPs, able to specifically detect antigen/antibody interactions with capability of preventing protein nonspecific adsorption.

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Study of antibody/antigen binding kinetics by total internal reflection ellipsometry

Cited by 58 publications

References 22 publications

Cancer biomarker discovery using DNA aptamers

Cancer biomarker discovery using DNA aptamers

Indirect competitive enzyme-linked immunosorbent assay of tris-(2,3-dibromopropyl) isocyanurate with monoclonal antibody

Nanostructured interfaces with site-specific bioreceptors for immunosensing

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