Surface plasmon resonance spectroscopic characterization of antibody orientation and activity on the calixarene monolayer

Chen, Hongxia; Huang, Junyi; Lee, Jaebeom; Hwang, Sungu; Koh, Kwangnak

doi:10.1016/j.snb.2010.03.033

Cited by 60 publications

(37 citation statements)

References 33 publications

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“…Previous results showed that bovine serum albumin (BSA) can be immobilized on three derivatives in a monolayer with different surface coverage [8]. Also, we confirmed the controlled antibody orientation on the Cal-4 crown SAM by surface plasmon resonance (SPR) study [11]. However, how surface conditions of Cal-4 derivatives affect the orientation of adsorbed antibodies is not well known.…”

Section: Introductionsupporting

confidence: 72%

Fabrication of Calix[4]arene Derivative Monolayers to Control Orientation of Antibody Immobilization

Chen

Liu

et al. 2014

IJMS

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Three calix[4]arene (Cal-4) derivatives which separately contain ethylester (1), carboxylic acid (2), and crownether (3) at the lower rim with a common reactive thiol at the upper rim were synthesized and constructed to self-assembled monolayers (SAMs) on Au films. After spectroscopic characterization of the monolayers, surface coverage and orientation of antibody immobilized on the Cal-4 derivative SAMs were studied by surface plasmon resonance (SPR) technique. Experimental results revealed that the antibody could be immobilized on the Cal-4 derivatives spontaneously. The orientation of absorbed antibody on the Cal-4 derivative SAMs is related to the SAM’s dipole moment. The possible orientations of the antibody immobilized on the Cal-4 derivative 1 SAM are lying-on or side-on, while on the Cal-4 derivative 2 and Cal-4 derivative 3 head-on and end-on respectively. These experimental results demonstrate the surface dipole moment of Cal-4 derivative appears to be an important factor to antibody orientation. Cal-4 derivatives are useful in developing site direct protein chips.

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Section: Introductionsupporting

confidence: 72%

Fabrication of Calix[4]arene Derivative Monolayers to Control Orientation of Antibody Immobilization

Chen

Liu

et al. 2014

IJMS

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“…The role of using a surfactant for negating formation of aggregates has previously been demonstrated by Choi and colleagues both for Protein A and Protein G complexes with IgGs [3,16]. In particular, they have investigated the effects of polysorbate (Tween 20) using atomic force microscopy and shown how the roughness of the surface was reduced by applying the surfactant.…”

Section: Application Of the Oriented Protein G Sensor Chipmentioning

confidence: 92%

“…Surface sensitive biosensors, such as surface plasmon resonance (SPR) and surface acoustic wave sensors, require elaborate design of the sensing surfaces in order to accomplish favourable orientation, high purity, long-term stability, and high activity of their capturing ligands [1][2][3][4]. By applying a primary layer of ligand on the surface with more than one capturing site, e.g., protein G or protein A, the orientation and purity can be enhanced and allow regeneration of a secondary capturing ligand [2,[5][6][7][8][9].…”

Section: Introductionmentioning

confidence: 99%

Orientation and capturing of antibody affinity ligands: Applications to surface plasmon resonance biochips

Bergström

Mandenius

2011

Sensors and Actuators B: Chemical

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A surface plasmon resonance (SPR) sensor chip with immobilized protein G was used for simultaneously capturing, purifying and orienting antibody ligands. The ligands were further stabilized by chemical cross-linking. This procedure of designing the sensor chip improved efficient use of the ligands and could prolong the analytical use.The procedure was evaluated on standard dextran-coated sensor chips onto which commercial semi-purified antibodies toward human serum albumin and human troponin where captured and used for analysing their antigens.The procedure demonstrates a general design approach for presenting the biorecognition element on a biosensor surface which enhances sensitivity, stability and selectivity at the same time as an impure ligand is purified.

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“…When surface bound, the asymmetrical dimensions of antibodies (14 Â 10 Â 4 nm 3 ) allow changes to the surface topography, i.e., film thickness and surface roughness, to be measured and can be representative of different antibody orientations. Chen et al 142 used AFM and SPR to confirm endon antibody orientation to the ProLinker TM SAM by plotting the height profile of the immobilized antibody and monitoring antigen uptake. Coppari et al 147 investigated a monoclonal antibody adsorbed on mica and, by combining height traces and images, were able to determine different antibody orientations with AFM.…”

Section: F Atomic Force Microscopymentioning

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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Surface plasmon resonance spectroscopic characterization of antibody orientation and activity on the calixarene monolayer

Cited by 60 publications

References 33 publications

Fabrication of Calix[4]arene Derivative Monolayers to Control Orientation of Antibody Immobilization

Fabrication of Calix[4]arene Derivative Monolayers to Control Orientation of Antibody Immobilization

Orientation and capturing of antibody affinity ligands: Applications to surface plasmon resonance biochips

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

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