MIT engineers have devised a way to pack antibody drugs into tiny, highly concentrated particles that can be pushed through a standard syringe. The advance could turn hours-long hospital infusions into quick injections, making lifesaving treatments easier to access.
For many people with cancer, autoimmune disorders or serious infections, treatment means hours in a hospital chair, tethered to an IV drip of antibody drugs. A new technology from MIT engineers points to a future where many of those same medicines could be given in minutes with a simple shot.
The team has developed a way to turn antibody solutions, which are usually too dilute and too thick to inject, into tiny solid particles suspended in liquid. Each particle is packed with antibodies at a concentration high enough that a full dose could fit into about 2 milliliters — the volume of a typical subcutaneous injection.
If the approach translates to the clinic, it could make powerful antibody therapies far more convenient and accessible, especially for people who struggle to get to infusion centers.
Lead author Talia Zheng, an MIT graduate student, noted that demographic shifts make this kind of innovation urgent.
“As the global population ages, making the treatment process more convenient and accessible for those populations is something that needs to be addressed,” she said in a news release.
The research is published in the journal Advanced Materials.
Antibodies in a bag, not a syringe
Therapeutic antibodies, such as rituximab for certain cancers, are large, complex proteins dissolved in water-based solutions. They are used to treat a wide range of conditions, from tumors and infectious diseases to autoimmune disorders like rheumatoid arthritis, inflammatory bowel disease and multiple sclerosis.
Today, these drugs are typically formulated at low concentrations — on the order of 10-30 milligrams of antibody per milliliter of liquid. That means a single dose can require at least 100 milliliters of fluid, far too much to push through a small needle into the tissue under the skin.
To shrink that volume to something injectable, drugmakers would need to raise the concentration roughly tenfold, to around 300 milligrams per milliliter or more. But when you try to simply concentrate existing formulations, the fluid becomes extremely thick and resists flowing through a syringe.
“You can’t concentrate existing formulations to these concentrations,” senior author Patrick Doyle, the Robert T. Haslam Professor of Chemical Engineering at MIT, said in the news release. “They’ll be very viscous and will exceed the force threshold of what you can inject into a patient.”
In 2023, Doyle’s lab showed that encapsulating antibodies in hydrogel particles could boost concentration, but that earlier method relied on centrifugation — spinning samples at high speeds — a step that is difficult to scale up for industrial manufacturing.
From emulsions to solid antibody particles
In the new study, the researchers took a different route that avoids centrifugation and is designed with large-scale production in mind.
They started by creating an emulsion, a mixture of two liquids that do not blend, similar to oil and vinegar. In this case, tiny droplets of a watery antibody solution are suspended in an organic solvent called pentanol.
Inside each droplet, the team added a small amount of polyethylene glycol, or PEG, a polymer commonly used in medicines and consumer products. PEG helps stabilize the antibodies as the droplets are dehydrated.
By carefully removing water from the droplets, the researchers were able to leave behind solid particles made almost entirely of antibody, with a concentration of about 360 milligrams per milliliter — higher than what is needed for most injectable formulations.
Once the solid particles formed, the surrounding pentanol was removed and replaced with an aqueous solution similar to the fluids currently used for IV antibody infusions: water with dissolved salts and a small amount of stabilizing polymer. The end result is a suspension of antibody-rich particles in a liquid that can still flow through a needle.
Crucially, the assembly process can be done rapidly using microfluidic devices — systems that precisely control tiny streams of fluid — and does not require centrifugation. That makes it more compatible with industrial emulsification equipment and good manufacturing practice (GMP) standards.
“Our first approach was a bit brute force, and when we were developing this new approach, we said to it’s got to be simple if it’s going to be better and scalable,” Doyle added.
Engineered to be injectable
To be useful in the clinic, the new formulations must not only be concentrated but also easy to inject.
The MIT team showed they could tune the size of the particles, from about 60 to 200 microns in diameter, by adjusting the flow rates in their microfluidic setup. For injectability tests, they focused on particles around 100 microns across.
Using a mechanical force tester, they measured how much force it took to push a syringe plunger filled with the particle suspension. The required force was under 20 newtons — well below what is generally considered acceptable for subcutaneous injections.
“That is less than half of the maximum acceptable force that people usually try to aim for, so it’s very injectable,” added Zheng.
With a standard 2-milliliter syringe, the researchers calculated that more than 700 milligrams of antibody could be delivered in a single shot. That dose range is enough for many existing antibody therapies.
The team also found that their formulations remained stable for at least four months when stored in a refrigerator, an important consideration for real-world use in clinics and pharmacies.
What comes next
So far, the work has focused on the physical formulation and injectability of the antibody particles, not on testing how well they work in the body. The researchers’ next steps include evaluating the therapeutic performance and safety of these formulations in animal models.
They are also working on scaling up the manufacturing process beyond the lab bench, using larger emulsification systems that could produce enough material for extensive testing and, eventually, human trials if the approach proves promising.
If successful, this technology could help shift many antibody treatments from hospital infusion centers to outpatient clinics, doctors’ offices or even at-home care, similar to how insulin and some biologic drugs are already given.
That shift would not only save time for patients and caregivers but could also reduce costs and ease pressure on health systems, especially as demand for antibody therapies continues to grow.