Immobilization of immunoglobulin-G-binding domain of Protein A on a gold surface modified with biotin ligase

Miyao, Hiroki; Ikeda, Yusuke; Shiraishi, Arata; Kawakami, Yuji; Sueda, Shinji

doi:10.1016/j.ab.2015.05.010

Cited by 19 publications

(20 citation statements)

References 25 publications

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“…73 and additional protein linkers. 103 The ZZ-domain has also been coupled to carbohydrate binding modules for selective immobilization to cellulose coated slides 104 and to paper 105 substrates, and also the metal affinity His-tag. 106,107 It is important to note that several issues may arise with such systems: (1) the Protein A capture of the Fc is reversible, (2) Protein A has been reported to bind Fab regions and albumin (although to a much lesser extent), and (3) it is required that the Fc binding site of the Protein A is correctly oriented at the substrate to permit antibody binding.…”

Section: Dna Directed Immobilizationmentioning

confidence: 99%

Orientation and characterization of immobilized antibodies for improved immunoassays (Review)

et al. 2017

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Orientation of surface immobilized capture proteins, such as antibodies, plays a critical role in the performance of immunoassays. The sensitivity of immunodiagnostic procedures is dependent on presentation of the antibody, with optimum performance requiring the antigen binding sites be directed toward the solution phase. This review describes the most recent methods for oriented antibody immobilization and the characterization techniques employed for investigation of the antibody state. The introduction describes the importance of oriented antibodies for maximizing biosensor capabilities. Methods for improving antibody binding are discussed, including surface modification and design (with sections on surface treatments, three-dimensional substrates, self-assembled monolayers, and molecular imprinting), covalent attachment (including targeting amine, carboxyl, thiol and carbohydrates, as well as “click” chemistries), and (bio)affinity techniques (with sections on material binding peptides, biotin-streptavidin interaction, DNA directed immobilization, Protein A and G, Fc binding peptides, aptamers, and metal affinity). Characterization techniques for investigating antibody orientation are discussed, including x-ray photoelectron spectroscopy, spectroscopic ellipsometry, dual polarization interferometry, neutron reflectometry, atomic force microscopy, and time-of-flight secondary-ion mass spectrometry. Future perspectives and recommendations are offered in conclusion.

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Section: Dna Directed Immobilizationmentioning

confidence: 99%

Orientation and characterization of immobilized antibodies for improved immunoassays (Review)

et al. 2017

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“…ZZ domains) captured the antibody more efficiently than single Z domain, suggesting multiple Ig binding domains may adopt a cooperative manner for Ig binding. [160] Ig binding via protein A or G is a non-covalent and reversible binding, which is good for protein A or G regeneration, thus improving their reusability. [161] However, the binding reversibility poses a problem for the stability of protein-antibody adduct that may not be suitable for certain applications.…”

Section: Antibody Immobilization Chemistriesmentioning

confidence: 99%

Site-selective orientated immobilization of antibodies and conjugates for immunodiagnostics development

Shen

Rusling

Dixit

2017

Methods

149

109

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Immobilized antibody systems are the key to develop efficient diagnostics and separations tools. In the last decade, developments in the field of biomolecular engineering and crosslinker chemistry have greatly influenced the development of this field. With all these new approaches at our disposal, several new immobilization methods have been created to address the main challenges associated with immobilized antibodies. Few of these challenges that we have discussed in this review are mainly associated to the site-specific immobilization, appropriate orientation, and activity retention. We have discussed the effect of antibody immobilization approaches on the parameters on the performance of an immunoassay.

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“…The BPL dimer was prepared by connecting the cysteine residues of two BPL molecules with a cross-linking reagent, 1,6-bis(maleimido)hexane. Here, a mutated BPL, BPL-Cys1, 26 which has a single cysteine residue, was used for the reaction. First, the cysteine residue of BPL-Cys1 was reduced by incubation with 20 mM DTT in HEPES (pH 7.5) containing 5 mM EDTA at 37 C for 90 min.…”

Section: Preparation Of Bpl Dimermentioning

confidence: 99%

“…All measurements were conducted at 25 C. Prior to measurements, the gold surface of the sensor chip was cleaned with piranha solution (3:1 mixture of sulfuric acid and 30% hydrogen peroxide) and then rinsed with distilled water. The mutated BPL, BPL-Cys2, 26 was immobilized on the cleaned sensor chip; BPL-Cys2 carries two cysteine residues which could be involved in binding to the gold surface of the sensor chip. Then, the Z-domain-containing polymers were prepared on the BPLmodified sensor chip with BZB and the BPL dimer.…”

Section: Spr Measurementmentioning

confidence: 99%

“…24,25 In a previous work, we succeeded in oriented immobilization of the antibody using fusion proteins of BCCP with the Z-domain, which were captured on the BPL-modified solid support. 26 Herein, we designed two types of engineered proteins to prepare the Z-domain-containing polymer on the solid support. One was the fusion protein of BCCP with the Z-domain (BZB), in which BCCP was genetically attached to the N-and C-termini of the Z-domain (Fig.…”

Section: Introductionmentioning

confidence: 99%

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Stepwise Preparation of a Polymer Comprising Protein Building Blocks on a Solid Support for Immunosensing Platform

2019

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In immunosensing, immobilization of the antibody on the sensing platform significantly influences the performance of the sensor. Herein, we propose a novel antibody-immobilization method based on a protein-polymer chain containing multiple copies of an antibody-binding protein, the Z-domain. In our approach, the Z-domain-containing polymer is prepared on the surface of the sensing platform with a biotinylation reaction from the archaeon Sulfolobus tokodaii. Biotinylation from S. tokodaii has a unique property by which biotin protein ligase (BPL) forms an extremely stable complex with its biotinylated substrate protein (BCCP). Here, we employed two types of engineered proteins: one was the fusion protein of BCCP with the Z-domain (BZB), in which BCCP was genetically attached to the N-and C-termini of the Z-domain; the other was a BPL dimer prepared by connecting two BPL molecules with a cross-linking reagent. We applied these two engineered proteins alternately onto the BPL-modified solid support of the surface plasmon resonance sensor chip, and succeeded in growing polymer chains comprising multiple units of BZB and the BPL dimer. The antibody-binding capability of the Z-domain-containing polymer thus prepared is adjustable by controlling the number of cycles of protein addition and the surface density of the polymer on the solid support.

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Immobilization of immunoglobulin-G-binding domain of Protein A on a gold surface modified with biotin ligase

Cited by 19 publications

References 25 publications

Orientation and characterization of immobilized antibodies for improved immunoassays (Review)

Orientation and characterization of immobilized antibodies for improved immunoassays (Review)

Site-selective orientated immobilization of antibodies and conjugates for immunodiagnostics development

Stepwise Preparation of a Polymer Comprising Protein Building Blocks on a Solid Support for Immunosensing Platform

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