It’s not surprising that the most important drug candidates and targets are super challenging when it comes to affinity screening. Immobilization-dependent techniques like SPR, and sample-consuming ITC struggle with demanding affinity screening applications such as ternary complexes, multimeric proteins, and intrinsically disordered proteins (IDPs). These are precisely the applications where Dianthus excels.


Dianthus is a plate-based, microfluidics-free screening platform that requires no surface immobilization, and measures under controlled equilibrium conditions – perfect for challenging affinity screenings. And not only that, Dianthus is a great choice if you’re looking for a complementary or orthogonal technique to validate hits and leads identified by other biophysical methods.

Lean on Dianthus when your affinity screening campaigns encounter roadblocks

Don’t give up just yet when you’re faced with a complicated affinity screening campaign. Armed with Dianthus, you have an opportunity to keep your project moving forward when your hit identification or lead optimization involves any of these molecules.

PROTACs and other small molecule protein degraders

Fragment libraries

Characterization of ternary complexes is tricky when you immobilize the preformed binary complex on a sensor surface. This is because the stability of the immobilized binary complex is compromised while you try to assess the affinity for your third component.

Dianthus measures under controlled equilibrium conditions that stabilize a binary target, while enabling you to characterize the ternary complex.

Additionally, it requires less assay development, less time, and less consumption of your target or small molecule when compared to SPR or FRET.

Because your method requires a significant change in mass to measure interactions, it’s difficult to identify hits from a library of fragments due to their very low molecular weight.

With Dianthus, you can identify hits from fragment libraries with confidence because measurements are mass-independent.

And, because Dianthus detects a broad range of affinity strengths, it’s useful for hit identification when fragments bind to proteins with mM affinity and lead optimization when fragments grow to form larger compounds that bind at low nM affinities.

Intrinsically disordered proteins (IDPs) and other aggregation-prone targets

Because IDPs don’t fold into a homogeneous 3D structure, you see aggregation triggered by non-native intermolecular interactions. On top of that, you are concerned with aggregation resulting from the high concentrations required by other methods.

With Dianthus, a high concentration is not required like it is with ITC. And if aggregation happens at low concentration, Dianthus differentiates between binding and aggregation so you get a better understanding of how the molecules behave.

Your method requires immobilization which easily disturbs the conformational equilibrium of IDPs.

Dianthus measures in solution, so the conformational equilibrium is not at risk of being disrupted as it happens with methods that require immobilization like SPR.

Large multicomponent complexes

DNA-encoded libraries

Assay conditions needed for immobilization to a solid surface are not allowing you to preserve the natural folding and quaternary structure of your multi-component complex involving protein-DNA or protein-protein complexes.

Dianthus measures under controlled equilibrium conditions — the perfect environment for stable multimeric complexes.

Because you’re concerned with false positives and want to ensure you’re selecting hits based on optimized drug-like properties, you’re looking for an affinity-based orthogonal method. Validating hit compounds from a DEL selection either by on-DNA (with DNA-tagged compounds) or off-DNA screening (when DNA tags are removed to avoid steric hindrance) is important.

Dianthus handles both on-DNA and off-DNA affinity screenings. And, large amounts of expensive tag-free compounds are not required for off-DNA analysis.

Learn how Dianthus characterizes ternary complexes formed by PROTACs, E3 ligases, and protein of interest


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Validate hits and leads with a well⁠-⁠established orthogonal technology

Looking to confirm hits identified with your primary technique or concerned you might be missing good ones? Researchers choose Dianthus for orthogonal validation, so they know which hits to move forward with. And it may also uncover other binders that were inaccessible to your primary method.

Read this publication to learn how hit fragments for MeK1 identified with TRIC correlate well with those found with SPR, MST, and TSA.

Beat common concerns encountered with technologies like SPR and ITC

There are common issues that worry most researchers as they embark on the planning of affinity screening campaigns. Relax and focus on your research knowing that with Dianthus you don’t have to fret about them.

Measure the broadest range of affinities
Dianthus detects a wide range of binding affinities — picomolar to millimolar — so you catch very strong and weak binders.

Characterize in solution, no immobilization required
Analyzing interactions in close-to-native conditions is ideal, especially when dealing with challenging targets. Dianthus characterizes in solution, so negatively impacting your target’s binding site or lacking control of the equilibrium conditions isn’t an issue.

Consume small amounts of target and compounds
Every little bit counts. Saving on costly sample and library compounds means you can do more screening or use them in other projects.

Learn how Dianthus helps characterize challenging drug discovery targets from 3 case studies.


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Dianthus is ready when you want to automate your affinity screening campaigns

When you incorporate Dianthus into an automated workflow, you get hours of uninterrupted and unattended operation. And the 384-well microplate format makes it compatible with many automation solutions. On top of that, Dianthus doesn’t require regular maintenance. Say goodbye to downtime and hello to access 24/7.

Dianthus NT.23PicoDuo

The most popular model when you need to identify hits with millimolar to picomolar affinities. And during lead validation measure ~ 1,500 Kds in 24 hours (12-point dilutions/Kd).

Dianthus NT.23Pico

Your best option if you want the capability of screening binding events with both millimolar and picomolar affinities to succeed.

Dianthus NT.23

Your solution if you know you’ll only need to screen binding events with nanomolar affinities.

Screen for hits and optimize leads based on affinity

Hit identification

Finding true hits faster is the most important step in making your drug discovery workflow efficient. With Dianthus, you’ll find hits quickly and move on to hit validation confidently, whether it’s fragment-based or small molecule single-dose screening.

Lead validation

Spend less time sorting through the strong and weak binders. Dianthus generates easy-to-interpret affinity ranking tables and histograms to help you quickly decide on the right candidates and start lead optimization sooner.

Lead optimization

Once validation is complete, it’s time to improve target specificity, selectivity, and potency. Use Dianthus to verify that binding affinities remain strong. This, combined with your ADME, toxicity, and PK/PD results, ensures you’re developing the best drug candidates.

See an example of fragment screening from a large chemical space with Dianthus


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Use proven technology that’s been around for over 10 years

Quantifying molecular interactions — measuring how tight or weak a ligand binds to its target — via Temperature Related Intensity Change (TRIC) isn’t new. It’s done by labeling your target molecule with a fluorescent dye and mixing it with your ligand. Then, a very precise and brief laser-induced temperature change is applied, causing a variation in fluorescence intensity which is amplified if your ligand binds to your target. This change in fluorescence is measured and plotted against your ligand concentration to obtain the dissociation constant or Kd.

Dianthus Technology

Decide which hits are worth moving forward with sooner

Generating results is great, but getting automated, actionable insights from your results is even better. Dianthus DI.Screening Analysis software gives you screening summaries as well as easy-to-interpret ranking tables and histograms. Quickly compare Kds and decide which candidates are worth moving forward with sooner rather than later.


Use high-quality consumables for fast hit screening

Get the high quality and consistency you expect from consumables when finding and validating hits. Dianthus 384-well plates have a proprietary coating that prevents protein from sticking to the wells, and they go through rigorous QC testing to ensure consistency from well to well. So, it’s no wonder the plate’s barcode helps you track your assay and data back to a specific plate. You’ll also want to use a 2nd Generation labeling kit — it labels your proteins or peptides with fluorophores selected for their sensitivity to binding events — so you get the best results.

If you’re looking to get your hit screening assay up and running quickly, use the Buffer Exploration Kit. The buffer plate provides a systematic approach to assay development — it’s pre-loaded with buffer systems that contain various salts, detergents, and additives. Simply mix any of these buffer combinations with your sample to quickly find the right buffer conditions. Finally, reduce the time and cost of assay development.

Use Dianthus for more than just affinity screening campaigns


Little did you know that Dianthus is capable of doing more than just hit identification and lead validation — like characterizing molecular interactions for a variety of applications.


Characterize binding events to understand biological processes and structure-function relationships

Support and confirm X-ray crystallography and Cryo-EM findings

Perform competition assays in the presence of inhibitors Learn more

Want to learn more about Dianthus?

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