French neuroscientist Philippe Rondard from CNRS in Montpellier hails camelid-derived nanobodies as a potential game-changer in neuroscience. “These tiny proteins could bridge the gap between large antibody drugs and small-molecule medications, opening exciting possibilities for brain disorders,” he explains.

A Tiny but Mighty Discovery​
Originally uncovered in the 1990s, nanobodies are unusual proteins found naturally in animals like llamas and camels. Unlike conventional antibodies, which have both heavy and light chains, these streamlined versions consist solely of heavy-chain fragments—making them roughly one-tenth the size of regular antibodies. Interestingly, this unique molecular structure appears exclusive to camelids and a few fish species.
While traditional antibody drugs have transformed treatments for cancer and autoimmune conditions, they’ve struggled to effectively target the brain. Even approved antibody therapies for neurological diseases, such as certain Alzheimer’s medications, often come with significant side effects.

Why Nanobodies Could Be Different​
Thanks to their compact size, nanobodies can more easily cross the blood-brain barrier—a major hurdle for most drug molecules. This enhanced access allows them to home in on neurological targets with greater precision, potentially reducing side effects while improving therapeutic outcomes. Early studies even demonstrated their ability to normalize behavior in mouse models of schizophrenia and related brain disorders.
“They’re highly soluble and can passively diffuse into the brain,” notes co-researcher Pierre-André Lafon. “That’s a stark contrast to many small-molecule drugs, which rely on lipid solubility to cross the barrier—often leading to poor targeting and unwanted reactions.”
Beyond their biological advantages, nanobodies are also easier to manufacture and modify than full-size antibodies. Scientists can fine-tune them to bind with exceptional specificity to neurological markers.

Challenges Before Human Trials​
Before these promising molecules can advance to clinical testing, several hurdles remain. Researchers must conduct thorough toxicity evaluations, assess long-term safety, and determine how long the nanobodies remain biologically active in the brain—key factors for establishing proper dosing.
“We also need to confirm their structural stability, proper folding, and that they don’t clump together,” Rondard emphasizes. “Developing stable, clinical-grade formulations that preserve their function during storage and transport is essential.”

Next Steps Toward Treatment​
Lafon reports that his team has already begun evaluating these factors in select brain-penetrating nanobodies. “Initial results suggest these molecules are compatible with long-term therapeutic use,” he says.
With their unique size, precision, and ability to cross the brain’s protective barrier, nanobodies may soon redefine how we treat neurological conditions.