Developability assessment
Rank candidates on how strongly they associate with themselves.
Self-interaction data sits next to SEC and dynamic light scattering in an early panel.
self-interaction
Protein aggregation assay, from self-interaction to active concentration
Knowing how much protein has aggregated is only part of the picture. A protein aggregation assay read as binding measures whether the remaining material is functional, how it self associates, and how much active protein remains.
Where protein aggregation analysis needs a binding readout
Label-free binding assays measures real-time binding of molecules. It adds a functional readout next to size and particle methods, covering the active concentration of a protein and how strongly a molecule associates with itself.
Formulation and buffer screening
Find the conditions that keep protein binding-competent.
Compare binding activity across buffers, alongside a nanoDSF thermal stability assay.
colloidal stability
Protein stability assay on stressed samples
Measure what still binds after applied stress.
Stress the material offline, then read activity at controlled analysis temperature.
stress testing
Immunogenicity and ADA
Characterize the antibody response to a biotherapeutic.
Kinetic ADA characterization next to a bridging ELISA titer.
anti-drug antibody
Amyloid and fibril research
Follow elongation on immobilized seeds in real time.
Binding kinetics next to ThT fluorescence and electron microscopy.
amyloid fibrils
Don't see your system?
Discuss your assay with one of our application specialists.
Talk to a specialist
Benefits of the inQuiQ in aggregation and stability work
01 / 04
One injection, four channels, sixteen sensors
Four addressable flow channels, four sensors each, with the sample passing through them in series.
30 µL minimumsequential flow paths
Put the molecule on the sensor and inject the same molecule
Self-association shows up as binding response, which ranks candidates on aggregation propensity before formulation work begins.
self-interactiondevelopability assessment
same molecule, both sides
Watch monomer add to an immobilized fibril seed
Amyloid-beta seeds are held on the sensor and monomer is injected over them, with the response recorded through the whole injection.
amyloid-betaseeded elongation
seed on surface, monomer in flow
Run a panel of candidates unattended
The inQuiQ768 autosampler takes 2×96 or 2×384 well plates and injects one sample after another, so every candidate meets the same surface.
2×96 wells2×384 wells
one plate, sequential injections
How an aggregate detection run works
Every sample follows the same five steps. A conformation-selective antibody is held on the sensor, the sample flows past, and the response is recorded through the whole injection. Assembled material binds; monomer does not.
Ligand immobilization
A conformation-selective capture antibody is coupled to the sensor surface.
It recognizes an epitope that only exists once subunits assemble. For amyloid-β that means oligomer and protofibril are captured while monomer is not.
- conformation-selective
- amine coupling
- assembled epitope
Deactivation
Unused activated sites are switched off before the first sample arrives.
Excipients, surfactant and carrier protein reach the surface with every injection. Deactivation, together with the antifouling hydrogel, keeps them out of the sensorgram.
- deactivation
- non-specific binding
- reference channel
Association
The sample is injected. Aggregate binds, monomer flows straight past.
Each aggregate is caught across several arms at once, so the surface loads quickly. The plateau reads assembled content rather than total protein.
- aggregate content
- multivalent capture
- label-free
Dissociation
Buffer replaces the sample and the response barely moves.
A multivalent complex has a very slow kd, so the captured material stays bound and only a small fraction releases. The signal that holds is what gets read across a stress timepoint series.
- slow kd
- complex stability
- stress timepoints
Regeneration
A regeneration buffer returns the sensor to baseline for the next sample.
Buffer alone will not clear an avidity-locked complex, so the surface is stripped deliberately. Every timepoint and every formulation then meets the same antibody layer.
- regeneration
- same surface
- unattended runs
Response (RU)
Time
What the inQuiQ does for aggregation and stability work
Six capabilities, one modular benchtop instrument, in a label-free workflow.
Self-interaction, measured directly
Immobilize the candidate and inject the same molecule. Weak self-association shows up as binding response, which ranks candidates on aggregation propensity.
self-interaction
developability
The same kinetic method at every stage
Binding kinetics are measured the same way in developability, formulation, and protein stability screening, so the binding affinity numbers compare across the workflow.
ka, kd, KD
Clean signal from serum and formulation buffers
The antifouling hydrogel limits binding by matrix and excipient components, with samples clarified through 0.22 µm before injection.
0.22 µm filter
Active concentration, not total mass
A standard curve of the reference material turns binding response into the concentration of protein that still engages its target.
standard curve
Orthogonal to size and particle methods
SEC, AUC, mass photometry, and light obscuration report how much aggregate is present. Binding data reports whether the rest still works, which is the functional half of biophysical characterization.
orthogonal characterization
Unattended runs on the inQuiQ768
The autosampler takes 2×96 or 2×384 well plates and works through candidate panels one injection after another.
2×96 wells
2×384 wells
Explore the inQuiQ768
Application notes, publications, and data
From small molecule kinetics to antibody affinity, explore real binding data generated on the inQuiQ. Each application note pairs a sensorgram with the affinity and kinetic values behind it.
Start A conversation
Talk to an application scientist
Bring your process step. We will tell you honestly whether label-free is the right method for it, and how the assay would be built.
Ready to see the inQuiQ in action?
Talk to an application scientist
Thirty minutes to discuss your assay design, before anyone mentions an instrument.
Download the inQuiQ brochure
Sensitivity, channel layout, footprint, and consumable formats in a couple of pages.
Delta Life Science
request@deltalifescience.nl
Send us an email, and we will get back to you as soon as possible.
request@deltalifescience.nl
Send us an email, and we will get back to you as soon as possible.
Questions researchers ask
Label-free binding analysis does not size or count aggregates. SEC, DLS, AUC, and light obscuration do that. What a protein aggregation assay adds is the other half of the question, namely how much of the material still engages its target and how strongly the molecule associates with itself. The two run alongside each other rather than one replacing the other.
Antibody developability is assessed on several axes, and binding data covers two of them: rank candidates on self-interaction and on retained target binding. A molecule that associates strongly with itself carries a higher aggregation and viscosity risk later in development, and a candidate that loses target binding under a formulation condition is telling you something a size profile will not.
Immobilise the molecule on the sensor and inject the same molecule as a concentration series. The response reflects how readily the protein binds to itself, which ranks candidates on aggregation propensity under a defined buffer condition.
It reports a change in binding behaviour rather than the presence of aggregate. Biphasic dissociation, poor fits to a 1:1 model, and a drifting maximum response all have several possible causes, including mass transport, surface heterogeneity, and ligand inactivation. Assign the cause with an orthogonal size method, then use the binding data to say whether the remaining material still works.
Apply the stress offline, whether that is heat, freeze-thaw, agitation or light, then inject the stressed material and the unstressed reference against the same capture surface. The instrument controls the analysis temperature, so a forced degradation study is compared under one set of conditions and differences in active concentration or in kon and koff can be attributed to the applied stress.
Capture the therapeutic on the sensor and inject patient or animal serum. The response gives a kinetic profile of the anti-drug antibody response, with kon, koff, and KD alongside the titer a bridging ELISA reports.