The resonant mirror: a novel optical biosensor for direct sensing of biomolecular interactions Part I: Principle of operation and associated instrumentation

Cush, R.; Cronin, J.M.; Stewart, William; Maule, C H; Molloy, J.; Goddard, Nick J.

doi:10.1016/0956-5663(93)80073-x

Cited by 402 publications

(187 citation statements)

References 14 publications

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“…Optical biosensor technology has been increasingly used to study molecular interactions [15,16], but almost all of these studies have involved plasmon resonance biosensors (BIAcore; Pharmacia). More recently, the resonant mirror bisensor [21,23] has been used to study the affinity of anti-saporin antibodies [20], and the kinetics of recombinant single-chain Fv binding to their antigens [24]. George et al have also been able to use the IAsys biosensor to detect and quantify the presence of human anti-mouse antibodies in the sera of patients treated with murine MoAbs [25].…”

Section: Discussionmentioning

confidence: 99%

“…George et al have also been able to use the IAsys biosensor to detect and quantify the presence of human anti-mouse antibodies in the sera of patients treated with murine MoAbs [25]. The advantages of biosensors include the ability to study molecular interactions in real time, with soluble proteins in their native state, undefiled by fluorescent, enzymatic or radio labels [21,23]. In this study, by coupling purified recombinant 3(IV)NC1 (the Goodpasture antigen) to the sensor surface, we have been able to examine the real-time binding of patients' autoantibodies.…”

Section: Discussionmentioning

confidence: 99%

“…Most biosensors used have employed surface plasmon resonance techniques to detect antibody binding. More recently, a resonant mirror biosensor (IAsys; Fisons Applied Sensor Technology, Cambridge, UK) has been developed to monitor molecular interactions quantitatively in real time [21].…”

Section: Introductionmentioning

confidence: 99%

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Epitope analysis of the Goodpasture antigen using a resonant mirror biosensor

Levy

Turner

George

et al. 1996

Clinical and Experimental Immunology

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SUMMARYWe have used a new technique for studying molecular interactions-a resonant mirror biosensor-to identify B cell epitopes within the Goodpasture antigen, which has recently been identified as the noncollagenous domain of the 3-chain of type IV collagen ( 3(IV)NC1). Recombinant antigen (r-3) was immobilized onto the sensing surface of a sample cuvette, and the binding of patients' autoantibodies or a MoAb to the Goodpasture antigen was followed in real time. All patients' sera bound r-3 in this system, while control sera did not bind. A MoAb inhibited the binding of all patients' autoantibodies to r-3, from 27% to 90% (mean inhibition 60%), and patients' sera cross-inhibited the binding of each other to the antigen. Binding was inhibited by pre-incubation of autoantibody with both native sheep 3(IV)NC1 and purified human 3(IV)NC1 monomers. Inhibition experiments using soluble overlapping peptides from human 3(IV)NC1 identified putative B cell epitopes. These results suggest that there is a major immunodominant epitope on the Goodpasture antigen, and that there is very limited heterogeneity in the autoantibody response in Goodpasture's disease. The resonant mirror biosensor can be successfully used to monitor antibody-antigen binding using polyclonal sera, and to map epitopes on autoantigens.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Epitope analysis of the Goodpasture antigen using a resonant mirror biosensor

Levy

Turner

George

et al. 1996

Clinical and Experimental Immunology

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“…Resonance mirror analysis [20] of the interaction between IDA peptides and the R-subunit was performed by using an IAsys cuvette system (Fisons). A cuvette with an aminosilane surface was washed with 10 mM sodium phosphate buffer (pH 7.7), and the surface was activated with 200 t.tl of 1 mM bis(sulfosuccinimidyl)suberate for 10 min, followed by extensive washing with sodium phosphate buffer.…”

Section: Resonance Mirror Analysismentioning

confidence: 99%

Biochemical evidence for the interaction of regulatory subunit of cAMP‐dependent protein kinase with IDA (Inter‐DFG‐APE) region of catalytic subunit

et al. 1996

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To explore the structural basis required for the hoioenzyme formation of cAMP-dependent protein kinase, we have prepared rabbit anti-peptide antibodies that can block the holoenzyme formation without affecting the catalytic activity of the enzyme. The antibodies were raised against a specific site in the catalytic (C)-subunit, termed IDA (Inter-DFG-APE) region, which lies between the kinase subdomains VII and VIII. Although the C-subunit immunoprecipitated with anti-IDA antibodies could not form a stable complex with regulatory (R)-subunit, it was still susceptible to inhibition by the R-subunit or by PKI, a specific inhibitor peptide containing a pseudosubstrate site. These results indicate that there exists an IDA regionmediated interaction between the R-and C-subunits, which is distinct from that mediated through the substrate site and substrate binding site. In accordance with this idea, association of synthetic IDA peptides with the R-subunit was directly demonstrated by resonance mirror analysis. The calculated association constants of IDA peptides were high enough to suggest a possible involvement of the IDA region in the initial step of holoenzyme formation.

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“…They are used in the real-time analyses of protein -protein interactions including the interactions between antigen/antibody, oligonucleotide/ oligonucleotide, protein/lipid, hormone/receptor and, also, drug/receptor -with the latter interactions being widely used for drug design and drug testing. OB techniques with resonant nanostructures-SPR [70] and RM [71] -take advantage, under total internal reflection conditions, of the evanescent wavelength as a probing element that registers refractive index changes occurring in the medium upon complex formation in the reaction zone limited to several hundred nanometres from the sensor surface. OB techniques enable to register complex formation of macromolecules with high concentration sensitivity (up to 10 212 M) and with time resolution of about a few seconds, providing the most convenient tools for studying macromolecules' complex formation in real time, for measuring association/dissociation rate constants as well as for determination of thermodynamic parameters of protein-protein complex formation.…”

Section: Obsmentioning

confidence: 99%

Nanotechnologies in proteomics

Ivanov

Govorun

Быков³

et al. 2006

Proteomics

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Progress in proteomic researches is largely determined by development and implementation of new methods for the revelation and identification of proteins in biological material in a wide concentration range (from 10 23 M to single molecules). The most perspective approaches to address this problem involve (i) nanotechnological physicochemical procedures for the separation of multicomponent protein mixtures; among these of particular interest are biospecific nanotechnological procedures for selection of proteins from multicomponent protein mixtures with their subsequent concentration on solid support; (ii) identification and counting of single molecules by use of molecular detectors. The prototypes of biospecific nanotechnological procedures, based on the capture of ligand biomolecules by biomolecules of immobilized ligate and the concentration of the captured ligands on appropriate surfaces, are well known; these are affinity chromatography, magnetic biobeads technology, different biosensor methods, etc. Here, we review the most promising nanotechnological approaches for selection of proteins and kinetic characterization of their complexes based on these biospecific methods with subsequent MS/MS identification of proteins and protein complexes. Two major groups of methods for the analysis and identification of individual molecules and their complexes by use of molecular detectors will be reviewed: scanning probe microscopy (SPM) (including atomic-force microscopy) and cryomassdetector technology.

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The resonant mirror: a novel optical biosensor for direct sensing of biomolecular interactions Part I: Principle of operation and associated instrumentation

Cited by 402 publications

References 14 publications

Epitope analysis of the Goodpasture antigen using a resonant mirror biosensor

Epitope analysis of the Goodpasture antigen using a resonant mirror biosensor

Biochemical evidence for the interaction of regulatory subunit of cAMP‐dependent protein kinase with IDA (Inter‐DFG‐APE) region of catalytic subunit

Nanotechnologies in proteomics

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