The use of regenerable, affinity ligand-based surfaces for immunosensor applications

Quinn, John; Patel, Pritesh; Fitzpatrick, Brian; Manning, Bernadette M.; Dillon, Paul P.; Daly, Stephen J.; O’Kennedy, Richard; Alcocer, Marcos; Lee, Heather; Morgan, Michael R. A.; Lang, Kenny

doi:10.1016/s0956-5663(99)00032-9

Cited by 58 publications

(40 citation statements)

References 24 publications

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“…For protein G this was noted as being critical for the amount of immobilized protein, as also previously reported [20]. Optimization was achieved by a pre-concentration in the dextran matrix, where a pH between 3.6 and 3.8 was found suitable for immobilization.…”

Section: Biosensor Surface Designmentioning

confidence: 54%

“…ranging from 1 to 3 10 -5 s -1 for the investigated concentrations. The estimations were obtained with a Langmuir isotherm fit and had residuals similar to those previously described for protein G [20].…”

Section: Biosensor Surface Designmentioning

confidence: 99%

“…Using orienting ligands for affinity binding of large analytes as whole cells is noteworthy. However, seems that this methodology is more apt for use with smaller analytes, such as proteins, where the sensitivity range of SPR is fully exploited [2,5,20,38]. Other methods of choice where the ligand orientation would favor the sensing mechanism could be the resonant mirror technique [39], optical waveguide lightmode spectroscopy [40,41] and dual polarization interferometry [42].…”

Section: Application Of the Oriented Protein G Sensor Chipmentioning

confidence: 99%

“…Protein G, in particular, has been shown to be useful in a variety of bioanalytical applications for efficient capturing and orientation of IgG antibodies for bacterial detection [16][17][18][19] in kinetic studies [20] and for IgG quantification in industrial applications [5]. Protein G is derived from group C and G Streptococcus, while protein A is from Staphylococcus aureus [21].…”

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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Section: Biosensor Surface Designmentioning

confidence: 54%

Section: Biosensor Surface Designmentioning

confidence: 99%

Section: Application Of the Oriented Protein G Sensor Chipmentioning

confidence: 99%

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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“…The use of Protein-A-or Protein-G-coated surfaces to immobilize immunoglobulin G (IgG), which is known to bind strongly to the Fc region in antibodies, would be an alternative approach. [41,42] A new class of the sitespecific/noncovalent immobilization technique has emerged. Winssinger and co-workers [43][44][45][46] and Lovrinovic et al [47] displayed a variety of molecules, including small molecules, peptides, and recombinant proteins, tethering oligopeptide nucleic acid (oligo-PNA) tags onto DNA microarrays through PNA-DNA hybridization.…”

Section: Surface Chemistry For Immobilization Of Capture Agents Onto mentioning

confidence: 99%

Protein‐Detecting Microarrays: Current Accomplishments and Requirements

2005

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The sequencing of the human genome has been successfully completed and offers the chance of obtaining a large amount of valuable information for understanding complex cellular events simply and rapidly in a single experiment. Interestingly, in addressing these proteomic studies, the importance of protein-detecting microarray technology is increasing. In the coming few years, microarray technology will become a significantly promising and indispensable research/diagnostic tool from just a speculative technology. It is clear that the protein-detecting microarray is supported by three independent but strongly related technologies (surface chemistry, detection methods, and capture agents). Firstly, a variety of surface-modification methodologies are now widely available and offer site-specific immobilization of capture agents onto surfaces in such a way as to keep the native conformation and activity. Secondly, sensitive and parallel detection apparatuses are being developed to provide highly engineered microarray platforms for simultaneous data acquisition. Lastly, in the development of capture agents, antibodies are now probably the most prominent capture agents for analyzing protein abundances. Alternative scaffolds, such as phage-displayed antibody and protein fragments, which provide the advantage of increasing diversity of proteinic capture agents, however, are under development. An approach involving recombinant proteins fused with affinity tag(s) and coupled with a highly engineered surface chemistry will provide simple production protocols and specific orientations of capture agents on the microarray formats. Peptides and other small molecules can be employed in screening highly potent ligands as well as in measuring enzymatic activities. Protein-detecting microarrays supported by the three key technologies should contribute in accelerating diagnostic/biological research and drug discovery.

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Proteins: Array‐Based Techniques

Tomizaki¹,

Usui²,

Mihara³

2008

Wiley Encyclopedia of Chemical Biology

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In recent years, array‐based technologies, including DNA microarrays and protein‐detecting microarrays have been getting more attractive and promising as high‐throughput research/diagnostic tools. DNA microarrays comprise oligo‐DNA immobilized onto solid surfaces. Whereas protein‐detecting microarrays are categorized in several formats depending on classes of capturing agents that selectively bind to proteins of interest. Protein‐based capturing agents such as antibodies and fusion proteins are commonly immobilized onto solid surfaces. Alternatively, DNA/RNA aptamers, synthetic peptides, and small molecules including drugs and carbohydrates also act as capturing agents. In particular, peptides as capturing agents are very versatile, because they are chemically prepared according to the well‐established standard synthetic procedures and enable site‐specific and directed surface modifications. In this review, we describe the basic features of protein‐detecting microarray technologies (capturing agents, surface chemistry, and signal generation/readout); thereafter we suggest that the use of synthetic peptides is a very promising and powerful tool to monitor not only protein–peptide interactions but also enzymatic activities.

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The use of regenerable, affinity ligand-based surfaces for immunosensor applications

Cited by 58 publications

References 24 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

Protein‐Detecting Microarrays: Current Accomplishments and Requirements

Proteins: Array‐Based Techniques

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