Study on orientation of immunoglobulin G on protein G layer

Bae, Young‐Min; Oh, Byung-Keun; Lee, Woochang; Lee, Won Hong; Choi, Jeong‐Woo

doi:10.1016/j.bios.2004.09.003

Cited by 134 publications

(58 citation statements)

References 33 publications

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“…1) has been carried out using spectroscopic ellipsometry [7]. This has shown the formation of IgG-Protein G complexes on gold chip in the order of 4 nm.…”

Section: Biosensor Surface Designmentioning

confidence: 99%

“…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]. By carrying out the orientation and purification of the candidate ligand antibodies simultaneously the need for purification prior to immobilisation is circumvented.…”

Section: Introductionmentioning

confidence: 99%

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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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“…1) has been carried out using spectroscopic ellipsometry [7]. This has shown the formation of IgG-Protein G complexes on gold chip in the order of 4 nm.…”

Section: Biosensor Surface Designmentioning

confidence: 99%

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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“…3b). It is known that molecules of protein G, immobilized as the first layer, promote the position of immunoglobulin normally oriented relative to the surface of sensor [11] (see Fig. 4a).…”

Section: Resultsmentioning

confidence: 99%

3D-quantification of biomolecular covers using surface plasmon-polariton resonance experiment

Chegel¹,

Chegel²,

Guiver³

et al. 2008

Sensors and Actuators B: Chemical

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3-D quantification of biomolecular covers using surface plasmonpolariton resonance experiment Chegel, V.; Chegel, Yu.; Guiver, Michael; Lopatynskyi, A.; Lopatynska, O.; Lozovski, V. Sensors and Actuators B 134 (2008) The concentration of surface molecules N s and components of molecular susceptibility jl (ω) can both be determined from surface plasmon-polariton resonance (SPPR) experiments, instead of effective layer thickness and index of refraction, which are usually determined. The theoretical consideration of a molecular layer as monolayer of separated 3D-oscillators provides a new perspective for investigating molecules during SPPR experiment. It is shown that SPPR response and the form of the reflective curve depend on the form of a biomolecule and its orientation relative to the surface of the metal-carrier of plasmon oscillations. The experimental data for immunological reaction for the calculation of surface molecular concentration and mass of biomolecular covering are presented.

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“…The glutaraldehyde solution may also be made slightly acidic to increase electrostatic repulsion between aminated particles [16] during the reaction and inhibit bridging/aggregation [17,18]. The result of this alternate protocol is that the antibodies are not oriented with the specific binding region outward [19]. As long as the target cells are Fc-blocked, however, this will not lead to nonspecific binding.…”

Section: Cerasome Functionalization With Antibodiesmentioning

confidence: 99%

Functionalization of Ceramic Liposomal Nanoparticles, Cerasomes, with Antibodies

Stamm¹,

Zha²

2012

J Phys Chem Biophys

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Study on orientation of immunoglobulin G on protein G layer

Cited by 134 publications

References 33 publications

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

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

3D-quantification of biomolecular covers using surface plasmon-polariton resonance experiment

Functionalization of Ceramic Liposomal Nanoparticles, Cerasomes, with Antibodies

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