Eikon Therapeutics, Inc. Common Stock 12th Annual Cantor Fitzgerald Global Healthcare Conference

Sure. Eikon is a late-stage therapeutics company. We have, right now, four main drug candidates in the clinic. Those include a TLR agonist, which is being developed for advanced melanoma and advanced non-small cell lung cancer. We also have two highly selective PARP1 inhibitors, one of which is brain penetrant and the other which is not brain penetrant. The not brain penetrant one is the most advanced, and is being developed for traditional indications, breast, ovarian, prostate, and perhaps some pancreatic activity as well. The brain penetrant molecule has similar options, but it also can be used in patients with active brain metastases. We also, beyond those three compounds, we have a highly selective Werner helicase inhibitor, which is in clinical trials as well. The most advanced studies are for our TLR agonist, which is in registration enabling studies for melanoma and non-small cell lung cancer. That's the oncology portfolio. The company is based on super-resolution microscopy, advanced imaging tools that permit us to evaluate targets that elude others and to prosecute targets that others simply can't pursue.

Over the long term, it's the most important source of value for the company.

That, however, is a minority of our expense because clinical trial expenses are significant for a late-stage company.

Right. Thanks. The entire reason why Eikon Therapeutics was started, why we started it, was to apply these advanced imaging tools, super-resolution microscopy, to drug discovery. Super-resolution microscopy has a long history. Eric Betzig, who helped to develop that field and shared the Nobel Prize for his discoveries in 2014, is the person who was a co-founder of Eikon Therapeutics. I got involved in this actually before he got the Nobel Prize a long time ago, more than 15 years ago, at the time when I met Eric. He explained that he had been working on a method that would permit us to look at individual proteins in living cells in a non-destructive way, and that could, in principle, permit us to evaluate how those proteins were behaving in living cells. The work was fascinating. When I was at Merck for my second tour of duty there, beginning in 2013, I had Eric come and spend time with our scientists.

He's a physicist by training, and he realized that by being able to evaluate what I'll call, in general terms, the motion of individual proteins in living cells, we could learn important things about the interactions of individual proteins, one with another. That turned out to be absolutely true, but in a way that surprised us. In order to make this work, we had to build instruments that permitted us to capture individual proteins that have been labeled with a fluorescent probe, and to watch them move around in living cells. Those tools took some time to build. We have quite a large engineering team. The instruments that we've built are entirely proprietary.

They permit us to evaluate millions of cells per day and typically 10 to 100,000 proteins per cell. We image at a rate usually of about 100 frames per second. We have roughly 10-millisecond time resolution for the motion of proteins in living cells, and roughly 10 to 30 nanometer, 10 to 30 billionths of a meter, spatial resolution for those proteins. What I say when I'm describing this to lay audiences, I say is what we're really studying is the social lives of proteins. It turns out that individual proteins have very rich social lives. They have friends and family, and they have family members that they like to see a lot of, and others, once a year at Christmas, would probably be okay. They have friendships that are deep and abiding, and others that are quite shallow.

We get to see them all, and we can see the partners. That turns out to be extremely powerful because biochemistry, of course, is a team sport. The motile characteristics of a protein are limited by the interactions of the protein that we have the label on with whatever it interacts with. Drugs typically influence the ability of proteins to interact with their friends and family. That is how they work. What that means is that you can screen for compounds that change motion, and what you find are compounds that change function. You can do that even if you do not know what the function is, as long as you have some kind of phenotype that you can measure.

What that means, of course, is that we can, as I say, we can prosecute targets that others would find impossible to prosecute. The data sets are enormously large because this is imaging data, again, that we are capturing in fractions of a second. We can work at frame rates that are higher than 1,000 frames per second. All I will say to you today is that little Eikon in Milpitas, California, is one of the largest data producers in the world. When our instruments are all running full tilt, which they often are, we produce on the order of a petabyte of data a day, which, as Russ Berman, our lead engineer, often says, is a ridiculous amount of data. A petabyte, just to give the scale, is roughly enough data to fill the U.S. Library of Congress 60 times per day. That is a lot of data.

Yeah. I think what we have demonstrated is that, as I said, we can identify potential targets because we can actually visualize them and we can see what happens as we interfere with them. We also do not really need to be structurally enabled in order to pursue a target, although often we become structurally enabled. We come to understand what the protein structure is and how it binds to a particular molecule that we would screen. Our screening assays are very fast. We can screen 1 million compounds or so in roughly 6 weeks. We can analyze those then using the same kinds of imaging tools. We sort of set a land speed record for our Werner helicase inhibitor, which went from the initial lead to a development candidate in about 16 months. That is, of course, in the clinic now.