Dual-Polarization Interferometry: A Novel Technique To Light up the Nanomolecular World

Escorihuela, Jorge; Martinez, Miguel A.; López-Paz, José Luis; Puchades, Rosa; Maquieira, Ángel; Giménez-Romero, David

doi:10.1021/cr5002063

Cited by 70 publications

(52 citation statements)

References 194 publications

(367 reference statements)

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“…The combined beams create an interference pattern that provides information regarding mass, film thickness, refractive index, and density. 138 Song et al 139 used DPI to investigate anti-PSA antibody (anti-PSA) immobilized covalently via lysines to thiolated DPI chips, or captured via the Fc using immobilized Protein G. The thickness of the two systems was monitored as the antibody bound the PSA antigen and a detection limit of 10 pg/ml was achieved. Song went on to investigate different methods for anti-PSA immobilization with DPI, comparing boronate chelation, TCEP reduction with maleimide covalent linkage, Protein G, and random immobilization methods to PEG:Thiol or amine modified DPI chips.…”

Section: B Spectroscopic Ellipsometrymentioning

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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Section: B Spectroscopic Ellipsometrymentioning

confidence: 99%

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

et al. 2017

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“…To measure the physical parameters of a layer deposited on the surface of a sensor chip, the AnaLight® Bio200 dual-polarization interferometer (Farfield Sensor Ltd, Salford, U.K.) was used [13]. A DPI sensor chip consists of two waveguides stacked one on top of each other.…”

Section: Dpi Measurements Of C4bmentioning

confidence: 99%

“…DPI measures the interaction between biomolecules in real time without the use of chemical tags by monitoring simultaneously the thickness, mass and density of a biological layer deposited on the surface of a sensor chip [13]. In the DPI instrument, this is achieved by the use of a sensing waveguide and a reference waveguide within the sensor chip, upon which a laser beam with two polarisations T E and T M is focused along its length (see Materials and Methods).…”

Section: Dpi Analyses Of Immobilised C4bmentioning

confidence: 99%

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Domain structure of human complement C4b extends with increasing NaCl concentration: implications for its regulatory mechanism

Fung

Wright

Gor

et al. 2016

Biochemical Journal

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During the activation of complement C4 to C4b, the exposure of its thioester domain (TED) is crucial for the attachment of C4b to activator surfaces. In the C4b crystal structure, TED forms an Arg 104 -Glu 1032 salt bridge to tether its neighbouring macroglobulin (MG1) domain. Here, we examined the C4b domain structure to test whether this salt bridge affects its conformation. Dual polarisation interferometry of C4b immobilised at a sensor surface showed that the maximum thickness of C4b increased by 0.46 nm with an increase in NaCl concentration from 50 to 175 mM NaCl. Analytical ultracentrifugation showed that the sedimentation coefficient s 20,w of monomeric C4b of 8.41 S in 50 mM NaCl buffer decreased to 7.98 S in 137 mM NaCl buffer, indicating that C4b became more extended. Small angle X-ray scattering reported similar R G values of 4.89-4.90 nm for C4b in 137-250 mM NaCl. Atomistic scattering modelling of the C4b conformation showed that TED and the MG1 domain were separated by 4.7 nm in 137-250 mM NaCl and this is greater than that of 4.0 nm in the C4b crystal structure. Our data reveal that in low NaCl concentrations, both at surfaces and in solution, C4b forms compact TED-MG1 structures. In solution, physiologically relevant NaCl concentrations lead to the separation of the TED and MG1 domain, making C4b less capable of binding to its complement regulators. These conformational changes are similar to those seen previously for complement C3b, confirming the importance of this salt bridge for regulating both C4b and C3b.

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“…It is well-known that QCM measurements do not permit the differentiation between the areal inertial mass of adsorbate and the retained liquid on flat surfaces, and it is often reported that QCM data analysis ''overestimates'' the areal inertial mass of adsorbate [1,6,[8][9][10]. Optical techniques such as ellipsometry [7,8,[11][12][13], reflectometry [14,15], surface plasmon resonance spectroscopy [16,17], and dual-polarization interferometry [18,19] have also been used to monitor adsorption of organic molecules independently of or in conjunction with QCM or a further development of QCM known as quartz crystal microbalance with dissipation (QCM-D). The use of an optical technique in tandem with QCM or QCM-D may allow for the determination of the adsorbate layer porosity [20][21][22].…”

Section: Introductionmentioning

confidence: 99%

The retention of liquid by columnar nanostructured surfaces during quartz crystal microbalance measurements and the effects of adsorption thereon

Rodenhausen

Davis

Sekora

et al. 2015

Journal of Colloid and Interface Science

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The areal inertial mass of structure-retained liquid varies linearly with nanostructure height. The proportionality constant is a function of the surface topography and agrees with the generalized ellipsometry-determined nanostructure film porosity, implying that nearly all intercolumnar liquid is retained. We report that for adsorption processes within porous nanostructured films, the quartz crystal microbalance is sensitive not to the combined areal inertial mass of adsorbate and retained liquid but rather to the density difference between adsorbate and liquid due to the volume exchange within the nanostructure film.

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Dual-Polarization Interferometry: A Novel Technique To Light up the Nanomolecular World

Cited by 70 publications

References 194 publications

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

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

Domain structure of human complement C4b extends with increasing NaCl concentration: implications for its regulatory mechanism

The retention of liquid by columnar nanostructured surfaces during quartz crystal microbalance measurements and the effects of adsorption thereon

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