Make your SPR workflow smoother, more efficient, and less costly with Tycho
In Surface Plasmon Resonance (SPR) assays, just like in any biophysical or biochemical experiment, it’s important to make sure the samples used are suitable for the job. Low quality proteins can lead to tedious assay optimization, hard-to-understand results, and the need for professional support to work out what’s wrong. Adopt Tycho into your routine to avoid these issues and become more productive.
Increase your SPR productivity at every step
by making sure your proteins are the best they can be
Be confident in your SPR results
Have you ever been puzzled by your data? Maybe you were expecting an interaction to be visible with SPR and it wasn’t, and it made you question the functionality of your interactants. Or maybe you followed the exact same protocol as always and got different results that left you confused. Tycho can show you whether your protein is functional, and whether your new protein batch is as good as the last one. Find out before you even start your experiment, so you don’t have to guess what happened.
Free up valuable time on the SPR system by speeding up your assay development
Use Tycho to figure out the best experimental conditions. A Tycho run only takes 3 minutes for up to 6 samples. With the insight gained from a Tycho run, you’ll get your SPR assays run faster, and you’ll need less time on the SPR system which frees it up for somebody else to use (or for you to run even more assays!).
Don’t pay for unnecessary troubleshooting
When you get questionable results, you may go looking for the problem in the SPR system. Getting help from the supplier is expensive and there isn’t always a fast resolution to the problem. Wouldn’t it be great to know if the sample is the issue rather than the SPR system? By using high quality, folded protein in your experiments, you can reduce the need for troubleshooting, and keep your costs and downtime low.
With Tycho, rest assured that your protein will perform. Choose the right running buffer, one that maintains the activity of your immobilized protein. This way, you get more out of each immobilization and spend less on sensor chips.
Make sure your proteins are functional for the whole assay
Often, you have to use low pH to immobilize your protein, but some proteins really don’t like low pH. Are you sure that your chosen conditions are optimal for maintaining activity of the protein and getting lots of data from one surface? Find out in 3 minutes which immobilization condition keeps your protein folded and ready to give you the best binding signal, before you even begin.
Avoid immobilizing unfolded protein
If you have more than a few potential binders to screen, you can run pre-screen thermal shift assay on Tycho. Move forward to your surface plasmon resonance assay only with those molecules that show an interaction.
Don’t waste your time on non-binders
How does Tycho identify sample quality?
Tycho verifies protein quality by looking at the structural integrity (or foldedness) of a protein. As a thermal ramp is applied, the changes in the intrinsic fluorescence, detected at both 350 nm and 330 nm, from tryptophan and tyrosine residues in the protein are measured. These changes in fluorescence signal indicate transitions in the folding state of a protein. The temperature at which a transition occurs is called the inflection temperature (Ti). The fluorescence is recorded during the thermal run, plotted as ratio and used to calculate Ti. Its initial value along with the change in signal over the run (Δ ratio) is also recorded.
Determine the right buffer recipe for your SPR assay
Use Tycho to identify the right buffer for every step of your SPR assay, for example the best pH for covalent immobilization of your protein on the chip surface. Not all proteins survive low pH conditions! Checking ahead of time whether your protein stays folded allows you to choose a condition that will immobilize your protein *and* keep it happy. You can check up to 6 conditions in one Tycho run, so 3 minutes is really all you need.
Confirm whether your protein (still) binds
Need to quickly see if there’s an interaction at all? Run a quick check with Tycho to find out if your protein interacts with another molecule – even another protein. There are many good reasons to do this: test your protein with your positive control analyte to confirm if it’s still functional after some time at room temperature, or in the presence of solvents like DMSO. Or, use it to identify and eliminate non-binders early, allowing you to focus your valuable SPR time only on the binders.
Verify similarity between batches
Got a fresh batch of protein? Want to know if it will perform like a “good” batch you’ve already worked with? With Tycho, compare the structural integrity of different batches to verify their similarity. This allows you to spot irregularities or contaminants before you proceed to your surface plasmon resonance assay. Working with high quality samples will result in more consistent SPR results that are easier to interpret and can be reported confidently.
Hit the bench running
Using Tycho is super easy — just follow the onscreen prompts to start an experiment. Assign names to your samples while your experiment is running to keep your records in order. When it’s done, simply export both the raw data, automatically analyzed results, and summary figures in a convenient ready-to-share format.
Explore the clouds with us
Tycho.Cloud offers advanced, cloud-based data analysis features for Tycho, like plotting and comparing your data across runs, automatically analyzing your thermal shift experiments, and more!
Anybody with access to a Tycho is invited to try out Tycho.Cloud. It’s still in beta, so it’s not perfect yet. Give it a whirl and help us build an awesome product.
Small amounts of sample is all you need
You can do so much (or so little) using Tycho and minute amounts of sample. Accurate results are obtained using tiny, precisely constructed glass capillaries so analysis can be done on virtually any sample type. No pipetting is required since sample is taken up by capillary force directly into the capillary, so you’re not wasting your precious sample.