The resonant mirror: a novel optical sensor for direct sensing of biomolecular interactions part II: applications

Buckle, Philip E.; Davies, Robert J.; Kinning, Tim; Yeung, Debra; Edwards, P. R.; Pollard-Knight, Denise; Lowe, Christopher R.

doi:10.1016/0956-5663(93)80074-y

Cited by 183 publications

(85 citation statements)

References 18 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%

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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%

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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“…Binary Interaction Analysis-Association and dissociation between HPG and the nSK/SK del254 -262 , referred to hereafter as binary interaction, were followed in real time by resonant mirror-based detection using the IAsys Plus TM system (Cambridge, UK) (27,28). In these experiments, streptavidin was captured on biotin cuvette according to the manufacturer's protocols (IAsys protocol 1.1).…”

Section: Kinetic Analysis Of Protein-protein Interactions Using Resonmentioning

confidence: 99%

Involvement of a Nine-residue Loop of Streptokinase in the Generation of Macromolecular Substrate Specificity by the Activator Complex through Interaction with Substrate Kringle Domains

Dhar¹,

Pande²,

Sundram

et al. 2002

Journal of Biological Chemistry

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The selective deletion of a discrete surface-exposed epitope (residues 254 -262; 250-loop) in the ␤ domain of streptokinase (SK) significantly decreased the rates of substrate human plasminogen (HPG) activation by the mutant (SK del254 -262 ). A kinetic analysis of SK del254 -262 revealed that its low HPG activator activity arose from a 5-6-fold increase in K m for HPG as substrate, with little alteration in k cat rates. This increase in the K m for the macromolecular substrate was proportional to a similar decrease in the binding affinity for substrate HPG as observed in a new resonant mirror-based assay for the real-time kinetic analysis of the docking of substrate HPG onto preformed binary complex. In contrast, studies on the interaction of the two proteins with microplasminogen showed no difference between the rates of activation of microplasminogen under conditions where HPG was activated differentially by nSK and SK del254 -262 . The involvement of kringles was further indicated by a hypersusceptibility of the SK del254 -262 ⅐ plasmin activator complex to ⑀-aminocaproic acid-mediated inhibition of substrate HPG activation in comparison with that of the nSK ⅐ plasmin activator complex. Further, ternary binding experiments on the resonant mirror showed that the binding affinity of kringles 1-5 of HPG to SK del254 -262 ⅐ HPG was reduced by about 3-fold in comparison with that of nSK⅐HPG. Overall, these observations identify the 250 loop in the ␤ domain of SK as an important structural determinant of the inordinately stringent substrate specificity of the SK⅐HPG activator complex and demonstrate that it promotes the binding of substrate HPG to the activator via the kringle(s) during the HPG activation process. Streptokinase (SK),1 a bacterial protein secreted by the Lancefield Group C ␤-hemolytic streptococci, is widely used as a thrombolytic agent in the treatment of various circulatory disorders, including myocardial infarction (1). Unlike other human plasminogen (HPG) activators, like tissue plasminogen activator and urokinase, SK does not possess any intrinsic enzymatic activity. Instead, SK forms an equimolar, stoichiometric complex with "partner" HPG or plasmin (HPN), which then catalytically activates free "substrate" molecules of HPG to HPN by selective cleavage of the Arg 561 -Val 562 peptide bond (2, 3). It is believed that consequent to the initial SK⅐HPG complexation, there is a structural rearrangement within the complex, and even before any proteolytic cleavage takes place, an active center within the HPG moiety capable of undergoing acylation is formed (3). This activated complex is rapidly transformed into an SK⅐HPN complex and develops an HPG activator activity. Unlike free HPN, however, which is essentially a trypsin-like protease with broad substrate preference, SK⅐HPN displays a very narrow substrate specificity (4). The structural basis of the conversion of the broadly specific serine protease HPN to a highly substrate-specific protease, once complexed with the "cofactor" SK, with exclusiv...

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“…Often touted as a label-free sensing technique, surface plasmon resonance based sensing and imaging have become commercially available for quite some time, and are employed in applications such as studying protein-protein interactions, immunochemical procedures and drug-receptor binding. Traditional surface plasmon resonance sensors rely on the propagating surface plasmon resonance (PSPR), where light-electron coupling is obtained via total-internalreflection, a condition typically achieved by prism coupling [3][4][5]. Due to the unconventional nature of light coupling, PSPR sensors face challenges in instrument miniaturization and simplification.…”

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confidence: 99%

3D Plasmonic Nanoarchitecture As an Emerging Biosensing Platform

Arnob

Shih

2017

Nanomedicine (Lond.)

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Propagating & localized surface plasmon resonanceRecent advances in plasmonics of coinage metals have attracted significant interest in the biosensing community [1,2]. Surface plasmon resonance refers to the oscillation of conduction band electrons excited by light. Often touted as a label-free sensing technique, surface plasmon resonance based sensing and imaging have become commercially available for quite some time, and are employed in applications such as studying protein-protein interactions, immunochemical procedures and drug-receptor binding. Traditional surface plasmon resonance sensors rely on the propagating surface plasmon resonance (PSPR), where light-electron coupling is obtained via total-internalreflection, a condition typically achieved by prism coupling [3][4][5]. Due to the unconventional nature of light coupling, PSPR sensors face challenges in instrument miniaturization and simplification. Another limiting factor for PSPR imaging is spatial resolution. Although, confined to the metal-dielectric interface, plasmon waves do propagate along the interface, therefore degrades spatial resolution.Localized surface plasmon resonance (LSPR) refers to nonpropagating plasmon modes identified in various nanostructures and colloidal nanoparticles [6]. In contrast to PSPR, LSPR provides the possibility of free-space light coupling and highly confined fields in all three dimensions, thanks to the nanostructures. These features can significantly reduce system complexity and measurement requirements [7]. In addition, since nanostructures are involved, the latitude of engineering design has substantially increased compared with PSPR where a thin film suffices. LSPR associated light concentration & field enhancementThe light concentrating property of LSPR is a focal point of modern plasmonic biosensing research. Typically understood as collective electron oscillation, LSPR produces highly localized electromagnetic field enhancement in plasmonic nanomaterials [6]. Plasmonic hot-spots refer to the locations, in close proximity of nanostructures, where electromagnetic fields are particularly enhanced relative to the incident field. LSPR associated local field concentration has been shown to enhance a variety of electronic as well as vibrational spectroscopic techniques. Among those, prominent examples can be drawn from Raman scattering, infrared and near-infrared (NIR) absorption and fluorescence [8][9][10][11].Traditional plasmonic nanomaterials are 1D (e.g., colloidal nanoparticles) or 2D (lithographically patterned nanostructure arrays) in nature, which typically result in sparse field concentration patterns. To improve efficiency and better utilization of hot-spots, the concept of 3D plasmonic nanoarchitecture, where abundant hot-spots are formed in a 3D volumetric fashion, have emerged [12]. Practically, there are several potential advantages of plasmonic sensing. First, many plasmonic sensing mechanisms can be implemented in a label-free fashion which requires no additional binding of fluorescent tag or radi...

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The resonant mirror: a novel optical sensor for direct sensing of biomolecular interactions part II: applications

Cited by 183 publications

References 18 publications

Epitope analysis of the Goodpasture antigen using a resonant mirror biosensor

Epitope analysis of the Goodpasture antigen using a resonant mirror biosensor

Involvement of a Nine-residue Loop of Streptokinase in the Generation of Macromolecular Substrate Specificity by the Activator Complex through Interaction with Substrate Kringle Domains

3D Plasmonic Nanoarchitecture As an Emerging Biosensing Platform

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