An antibody-like compound known on land to be exclusively to be found in camelids like alpacas, lamas, and dromedaries, could be used to treat human brain disorders such as Alzheimer’s disease, according to a new study.
The study’s focus were antibody-like proteins, aptly called nanobodies, whose small size allowed the scientists to treat neurological conditions in mice more effectively and with fewer side effects.
The study, published in the journal Trends in Pharmacological Sciences, outlines the next steps towards developing nanobody treatments that are safe for humans.
“Camelid nanobodies open a new era of biologic therapies for brain disorders and revolutionize our thinking about therapeutics,” said Dr. Philippe Rondard, of Centre National de la Recherche Scientifique (CNRS) in France.
“We believe they can form a new class of drugs between conventional antibodies and small molecules.”
Nanobodies were first discovered in the early 1990s by Belgian scientists studying the immune systems of camelids. They found that as well as making conventional antibodies, which are composed of two heavy chains and two light chains, camelids also produce antibodies with just heavy chains.
The antigen-binding fragments of those antibodies are now known as nanobodies. They’re just one-tenth the size of conventional antibodies, and have not been found in any other mammals, say scientists, although they have been observed recently in some cartilaginous fish.
Therapeutic approaches for diseases such as cancer and autoimmune disorders often centre around antibodies. The treatments that have shown some therapeutic benefits, including a few drugs for Alzheimer’s treatment, are often associated with secondary side effects, however.
With their much smaller size, scientists say nanobodies have the potential to offer better efficacy for brain diseases with fewer side effects. In previous studies, the team has shown that nanobodies can restore behavioral deficits in mouse models of schizophrenia and other neurologic conditions.
“These are highly soluble small proteins that can enter the brain passively,” said co-author Dr. Pierre-André Lafon, also of CNRS. “By contrast, small-molecule drugs that are designed to cross the blood-brain barrier are hydrophobic in nature, which limits their bioavailability, increases the risk of off-target binding, and is linked to side effects.”
He says nanobodies are also easier than conventional antibodies to produce, purify, and engineer and can be fine-tuned to their targets.
But the researchers acknowledge that several steps need to be taken before nanobodies can be tested in human clinical trials for brain disorders. They say toxicology and long-term safety testing are essential, and the effect of chronic administration needs to be understood.
“It will be necessary to obtain clinical-grade nanobodies and stable formulations that maintain activity during long-term storage and transport,” said Dr. Rondard.
Dr Lafon added that his lab has already started to study these different parameters for a few brain-penetrant nanobodies and has recently shown that conditions of treatment are compatible with chronic treatment.”
This article by Andy Corbley was first published by Good News Network on 10 November 2025. Lead Image: Credit, Sung Jin Cho on Unsplash.
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