A generation of drugs called monoclonal antibodies, also known as MABs, is altering the landscape of disease treatment by selectively targeting disease-causing agents and kick-starting immune cells. Using space-like conditions for further research may reveal ways to make drugs more targeted, concentrated and easier to administer.

MABs make up about one-third of protein-based therapeutics and are most often used to treat cancer and inflammation. They are widely regarded for their ability to target the specific protein of a pathogen and stop it from invading more cells. This means the therapy is tailored to the patient’s disease. The problem, however, is that patients need to get these drugs in large quantities over extended periods of time.

Proteins are too small to study under a microscope, so growing them into crystals lets researchers get a better understanding of their 3D constitution. Their makeup reveals how each protein works and how it contributes to disease scenarios. Once we understand this, drugs can be developed that mesh with the protein and fight the disease.

As well as being an important category of therapeutics, proteins are themselves drug targets. Drug companies need high-resolution protein structures to design suitable drugs.
This is where microgravity comes in.
Earth’s gravity can inhibit the growth and quality of crystals by affecting how the molecules position themselves on the exterior of the crystal. This makes space or a space-like environment ideal for this type of research.

AN INVOLVED PROCESS

David Sheehan, professor of biochemistry at Khalifa University, has been working on a method of crystalizing proteins for 12 years. His proteins are awaiting the arrival of vacuum chambers that mimic microgravity in a collaboration with Sean Shan Min Swei of the Department of Aerospace Engineering.

While turning proteins into crystals might seem like a cool magic trick, the process is quite involved. And many of the victories in successful crystallization can be attributed to time, patience and a lot of luck.

CAPTION: Crystals of protein furin grown on earth

Sheehan says initially, the protein is purified or separated from anything that might inhibit crystallization, like fatty materials from cells. The pH level is maintained for an optimum growth environment, and salt might be added to increase the ionic strength — or concentration — of the solution.

Other precipitants like polyethylene glycol or organic solvents, which decrease the protein solubility, are added. Then, the conditions are manipulated in a variety of ways, such as adjusting the temperature or exposure to gravity.

“The chemical additives and pH combined make up a condition. Most proteins only give crystals in a small number of conditions, so it is necessary to screen thousands of conditions to find the small number that will yield usable crystals,” Sheehan tells KUST Review.

And then it’s a waiting game — crystals might form in a week, a year or not at all.

Sheehan says researchers spend most of their time watching and hoping for a crystal, but most won’t see it: “When and if a crystal appears, then you’ve got a project.”

In his case, the crystals responded well to the addition of nanoparticles. While most of these types of experiments might typically result in one or two crystals from thousands, Sheehan’s team grew 15 crystals out of a panel of 16 proteins studied.

“We found one formulation that worked better than the others. So, then we used that nanoparticle with about 200 conditions,” he tells KUST Review.

This is unheard of, he says. And he knew they were on to something significant.

JOURNEY TO MICROGRAVITY

The project has a long history.

Sheehan grew his first nanoparticle-doped protein crystal over a decade ago, the result of an idea that had been brewing, a fridge full of available proteins, a student looking for a project and a friend with access to a synchrotron, a machine that uses electricity to create intense X-ray beams to study matter’s chemical and structural properties.

The student experimented with two nanoparticles, different from the ones used on the recent project: “The crystals grew very quickly and in the presence of a nanoparticle, they were larger, they grew faster, and they really grew. And that worked with both nanoparticles,” he says.

The stars (or crystals rather) aligned, and Sheehan and his student were soon transporting proteins to Dublin to a crystallographer friend who agreed to take them to the Paris synchrotron.

A synchrotron is about the size of a football field and is an ideal way to determine the three-dimensional atomic structure of a protein. It generates very intense X-ray beams that pass through a protein crystal and are scattered by the protein’s electrons.

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The crystal is rotated and a second scatter pattern is obtained. From these scatter patterns an atomic level structure can be calculated, Sheehan says.

FOCUS ON PROTEINS

But why are we so focused on proteins? Why not other molecules?

Proteins are the worker bees of a cell. They play an essential role in most biological systems and are responsible for most cellular functions. They are responsible for the shape, the interior design, production, cleanup, general upkeep and communication of cells. This makes them of great interest for targeted drug development, Sheehan says.

There are more than 130 protein-based therapeutics on the market, and the next step is to make them even better.

Current drugs for diseases like cancer, for example, require patients to take them for lengthy periods. Patients might sit in a clinic, hooked up to an IV for hours at a time, to ensure they get the right concentration of treatment. These treatments can go on for months or years. Imagine if patients could receive a simple injection in a doctor’s office.

And this type of drug development is dependent on research like that of Sheehan and his team.

Furin, for example, is a potential antiviral drug target for treating COVID-19.

Aside from the contributions to science, fighting disease and improving patient care, it could also mean a commercial venture.

“This could be very big,” Sheehan says. “I can see two options for commercialization, one of which is to market this as a crystallization screen and the other a start-up offering this as a service to pharmaceutical companies, biopharma and scientists around the world who have proteins they want to structure.”

With the team’s current success rate of more than 90 percent, it’s promising.

Sheehan and his researcher Salma Sultana Syed have patented their screen in the USA, UAE and Europe. They are exploring creating a start-up to be called ProScreenix. after incorporating a vast number of additional proteins into their research and changing up the nanoparticles using their current screen. This will create a more difficult problem, but test the method against a more robust array of challenges and hopefully improve the success rate. If you can’t take your proteins to space, bring space to your proteins.

Success is also dependent on microgravity, so Sheehan’s team will use space-simulation chambers that mimic these conditions, offering faster crystallization time and higher quality crystals.

The team is also hoping to acquire a robot that will help increase the number of conditions from 160 to approximately 1,000 and increase the number they can test daily. “At this point, when you get to that stage, you’re in the zone of talking about having a center for excellence,” Sheehan says.

Now they just need the right investors.

According to Allied Market Research, the protein therapeutics global market value is expected to reach U.S.$566.6 billion by 2030, up from U.S.$283.64 billion in 2020.

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