Revolutionize Your Screening Workflow with GCI: Fast, Accurate, Label-Free Kinetics and Affinities
Grating-Coupled Interferometry (GCI) is a game-changer for high-throughput screening (HTS), offering unparalleled speed and sensitivity compared to other surface-based kinetic techniques like SPR. 2bind’s advanced WAVEdelta system, with its unique waveRAPID mode, delivers rapid kinetic binding analysis, allowing you to quickly identify promising compound or even fragment hits and optimize lead compounds. Our expert team is dedicated to designing and executing tailored GCI screening campaigns that meet your specific requirements, ensuring you get the high-quality data and actionable insights needed to accelerate your drug discovery process.
GCI's strength lies in its ability to quantify molecular interactions without the need for labels or tags, preserving the native state of biomolecules. This label-free approach streamlines experiments, reduces costs, and minimizes the risk of interference.
In contrast to traditional surface-based kinetic methods like SPR, in GCI, every photon traverses the entire waveguide/sensor chip, collecting signals from a multitude of interactions. This amplified signal detection translates to inherently higher sensitivity compared to other methods. Additionally, the waveguide's design minimizes interference from changes in the bulk solution, ensuring accurate and reliable measurements. Thus, the WAVEdelta system, powered by GCI, delivers exceptional sensitivity and throughput.
The unique waveRAPID screening mode enables rapid kinetic characterization, ideal for high-throughput screening and optimization studies. By quickly identifying promising drug candidates or optimizing biotherapeutic molecules, you can significantly accelerate your research timeline. Due to the exceptionally high sensitivity, the waveRAPID screening mode even works with fragment libraries!
Association rate constant. Provides information on how fast complexes form; can be used for KD determination.
Dissociation rate constant. Provides information on how fast complexes dissociate; can be used for KD determination.
Equilibrium dissociation constant. Can be obtained by kinetic or classical equilibrium binding analysis. Provides information about the strength but not the dynamics of an interaction.
Binding enthalpy. KD values at different temperatures can be used to obtain the binding enthalpy of an interaction via van't-Hoff-plots.
Equilibrium dissociation constant. Can be obtained by kinetic or classical equilibrium binding analysis. Provides information about the strength but not the dynamics of an interaction.
At 2bind, our team of GCI experts has a proven track record of delivering high-quality data and insights to our clients. We work closely with you to design custom experiments, analyze data, and provide expert interpretation to ensure your research goals are met. Partner with 2bind to harness the full potential of GCI and drive your life science research to new heights.
Drug Discovery: Identify and validate drug targets, assess drug efficacy, and optimize lead compounds.
Screening: Quickly screen fragment and compound libraries with full kinetic profiling of hits
Biotherapeutic Development: Characterize antibody-antigen interactions, monitor biosimilar comparability, and optimize formulations.
Academic Research: Investigate fundamental biological processes, study protein-protein interactions, and explore novel therapeutic targets.
Traditional SPR sensors, gold-coated glass slides, rely on exciting surface plasmons with polarized light. This generates an evanescent wave (electromagnetic field) that detects changes in refractive index caused by molecular interactions. However, SPR faces limitations: A complex setup (SPR systems require intricate fluidics and detection arrangements), a limited detection area (the evanescent wave field restricts the detection zone), and “invisible” interactions (binding events outside the evanescent field go undetected).
Waveguide interferometry, employed in the WAVEdelta GCI system, also measures refractive index changes. However, it uses a waveguide structure to create an evanescent field spanning the entire sensor surface. This enables detection of binding events across the whole surface, offering distinct advantages over SPR: Enhanced Sensitivity (significantly greater due to signal detection across the full sensor), whole-surface detection (captures all interactions, not just those within a limited field), reduced interference (a shallower evanescent field minimizes bulk refractive index artifacts), and improved signal-to-noise ratio (clearer signals for more accurate data interpretation). By overcoming the limitations of SPR, GCI-powered waveguide interferometry with the WAVEdelta system delivers a powerful tool for high-quality, label-free analysis of molecular interactions.
All common immobilization strategies used for SPR are available also for GCI: Amine-coupling, Capture-coupling, Ni-NTA-coupling, Streptavidin capture, Neutravidin capture, and others.
Association rates constants range from 103 to 5·107 M-1s-1 for small molecules and 103 to 3·109 M-1s-1 for large molecules. Dissociation rate constants can be measured in the range between 10-5 and 10 per second.
Analyte:ligand molecular weight ratios up to 1:1000 are possible.
Absolutely. By combining the microfluidics and the biosensor in a single disposable cartridge, the WAVEdelta system offers crude-sample robustness normally only achieved with plate-based assays. Compatible biofluids include 100% serum or plasma, cell lysates, crude membrane preparations, large drug targets, virus-like particles (VLPs), liposomes, and aggregates (fibrils); all without the risk of clogging the system.
GCI offers a unique combination of advantages for molecular interaction analysis. Its clog-free design allows for the analysis of large molecules, aggregates, and even viscous samples without interruption. GCI’s flexibility extends to a wide range of sample conditions, enabling exploration of diverse solubilization and purification options for membrane proteins, including detergents and solvents. Researchers can also gain real-world insights by assessing drug performance in complex biological matrices like undiluted human serum and plasma. GCI’s broad applicability is further demonstrated by its ability to screen, rank, and characterize a wide range of analytes, from small molecules and fragments to weak binders with fast dissociation rates. High-affinity interactions are not a challenge for GCI, as it accurately measures the kinetics of tight binders with low dissociation constants (KD). With the capacity to quantify binding affinities across a broad range from picomolar (pM) to high micromolar (µM), GCI delivers confident and comprehensive kinetic analysis. This versatility, coupled with high sensitivity and throughput, makes GCI an invaluable tool for accelerating research and gaining deeper insights into the intricacies of molecular interactions.
