Proteins are incredibly versatile in the human body. Among many other things, proteins are the enzymes that help digest our food, the catalysts that cause our muscles to contract and release, the carriers of oxygen through the bloodstream, and the hormonal chemical messengers that regulate some of our most vital body processes.
Special proteins called antibodies bind to bacteria, viruses, and other harmful cells and substances in the body. They flag these invaders so the immune system can easily find and destroy them.
But antibodies aren’t interchangeable: each one has a unique shape and chemical makeup, and it can only recognize and bind to certain substances. Some diseases, such as certain types of cancers and infections, tend to slip past the body’s natural defenses because a person’s antibodies often don’t recognize them.
So what if you could custom-design antibodies to bind to some of these trickier pathogens and activate the immune system? Olivia Rissland, PhD, a professor of biochemistry and molecular genetics within the University of Colorado Anschutz School of Medicine, is designing a sophisticated tech platform that could allow scientists to do just that.
This research was recently selected for a 2026 CU Anschutz SPARK Award, from CU Anschutz Innovations. These grant bridge the gap between academic discovery and the clinic through product development-based funding and hands-on advising from industry experts.
Proteins are made from a cell’s RNA. Normally, after a new protein forms, it separates from the RNA that was used to create it, which is a barrier to custom protein design. By solving this barrier, Rissland’s platform lets researchers use customized, lab-created RNA to make proteins and identify which version of the protein works best.
“What that means is you can do all kinds of biochemistry on all these slightly different proteins, and you can ask which one is better,” she says. “And then you can identify its RNA instruction manual so you can make more of it.”
How proteins are made
Cells throughout the body are constantly in the process of making proteins. As older proteins degrade and break down, new ones are made to replace them.
A protein is made up of a long chain of amino acids joined together via peptide bonds. Each peptide chain gets bent and twisted into a unique 3D shape based on the combination of amino acids in it. The shape and chemical makeup of the protein determines how it will function in the body.
Although there are only 20 different amino acids, the body assembles these building blocks like molecular letters to make a protein. Two chains with the exact same amino acids but in a different order will create two different proteins. Rissland says an average protein can have a peptide chain that’s 600 amino acids long — so that adds up to roughly 20 to the 600th power different proteins that can be made.
Proteins are assembled through an intricate process inside cells. First, genetic instructions from the cell’s DNA are copied and transcribed to a strand of messenger RNA (mRNA). The mRNA travels to a specialized organelle called a ribosome, which reads the mRNA and ultimately translates it into a peptide chain. Once the chain leaves the ribosome through a protected tunnel, it folds into its final 3D shape and becomes a full-fledged protein.
Ribosomes consume over 60% of the total energy used by a cell. Each cell in the human body can have millions of ribosomes. And normally, once a ribosome has done its job, it disassembles, leaving the protein and the RNA to drift apart and do their separate functions. The ribosome can reassemble when it’s needed again.
The key to Rissland’s platform is a protein she and fellow researchers discovered that acts as an “anchor” and keeps cellular proteins, RNA, and ribosomes stuck together in clusters. With the RNA attached, it’s much easier for the researchers to determine the genetic makeup of the proteins they’re studying.
Rissland suggests thinking of each RNA strand as a recipe in a cookbook that explains how to make a specific dish, such as peach pie. She imagines herself as a judge in a peach pie competition, sampling many different recipes before stumbling on the best one.
“Once you find the best peach pie, you'd like to know what the recipe was that made it. So you need some way of connecting the pie and the recipe. That's very easy for us to do when we are working with pies, but it's much harder to do with molecules,” Rissland says.
“Essentially, our platform makes a durable connection between the peach pie and the recipe. So we can do all the tasting on the peach pie, we can find our winner, and along with it comes the recipe so we can make more of it.”
Future potential
Rissland and her team are still developing the platform, but she plans to eventually use the technology to engineer customized proteins, and she sees possibilities for numerous different applications.
For example, Rissland says, these customized proteins could be used to block molecules in the blood that trigger inflammatory bowel conditions like Crohn’s disease. The platform can also allow researchers to create and test proteins that are stable and won’t degrade in the bloodstream.
“Our system is really robust, and so we're going to be able to have many different types of applications,” she says. “And we can use it for peach pie, but we could also use it for blueberry pie. We could use it for lasagna. We could use it for salads. In some sense, it doesn't matter what the recipe is making. What our system allows us to do is to keep the recipe with the dish that was made, no matter what it was.”
