Science currently offers supportive care for Creutzfeldt-Jakob disease (CJD), as there is no therapy capable of stopping or reversing the condition. However, for the first time in the history of the disease, drug candidates that act directly on its mechanism are being tested.
The Leopoldo de Meis Institute of Medical Biochemistry at the Federal University of Rio de Janeiro (UFRJ) is involved in one of these studies, which is still in the preclinical phase. It is important to emphasize that no tea, capsule, extract, or plant supplement has the capacity to treat CJD.
CJD is caused by prions, which are abnormal forms of a protein produced by the body itself, and not by viruses or bacteria. When this protein undergoes structural alteration, it induces other normal proteins to change shape in a chain reaction, leading to the accumulation of abnormal forms and brain impairment.
This disease is considered rare, affecting about one to two cases per million inhabitants annually. Most cases are sporadic, without an identifiable source of infection, and are not transmitted through daily contact. This differs from the variant of CJD linked to the 'mad cow' epidemic, where acquiring the disease does not imply consuming meat.
One investigated approach aims to reduce the raw material needed for the production of new prions. ION717, an antisense oligonucleotide, interferes with the cellular message responsible for producing the prion protein. The Ionis trial had 56 participants in 2024 and started a new arm in March 2026, with results expected only in 2027.
In April 2026, a second strategy, PRiSM, entered trials. This uses small RNA (siRNA), administered via lumbar puncture, to decrease the production of the prion protein. It is a Phase 1 study involving 15 symptomatic patients, conducted by the Broad Institute in collaboration with UMass Chan, focusing on safety and tolerability.
Additionally, there is a randomized, placebo-controlled trial registered in China that evaluates efavirenz, an antiviral drug against HIV, which has shown prolonged life in infected mice, but recruitment has not yet begun.
Neither of the first two studies is recruiting participants in Brazil, and none of these methodologies have managed, so far, to halt the progression of the disease in humans. Drugs such as quinacrine, doxycycline, flupirtine, and a monoclonal antibody, used under special license in the United Kingdom, have also been tested without altering the course of CJD.
What has changed in the scientific landscape is the nature of the molecules being tested: they are now designed to act on the central mechanism of the disease, showing proven efficacy in animal models.
Another question raised is what to do with the existing protein aggregates at the time of diagnosis, given that the disease progresses rapidly. Therefore, research seeks molecules that can prevent the formation of new aggregates and, ideally, destabilize those that have already formed.
In a study conducted by UFRJ, in partnership with the Fluminense Federal University and the Federal University of Goiás, an article was published in an international journal describing the use of Moringa oleifera, commonly known as white acacia, as a natural library of molecules. The investigation did not start from the premise that moringa would cure prions, but rather whether any substance from the plant would interact with the prion protein.
Two compounds were identified, chlorogenic and neoclorogenic acids, which bound to the protein and, in in vitro assays, reduced the formation and disorganized established aggregates. This finding has two relevances: methodological, as it allowed isolating binding molecules directly from a crude extract without long chemical fractionation processes, and the disaggregation effect, crucial for treating symptomatic patients.
However, before any discussion of treatment, it is essential to prove the effect in cells and animals, determine the concentration that reaches the brain, and understand what happens after the disaggregation of an aggregate.
In Brazil, there has been a concrete advance with the RT-QuIC test, available at the UFRJ laboratory, which can detect the conversion of the prion protein in cerebrospinal fluid, confirming the diagnosis while the patient is still alive.
Sporadic CJD usually occurs between the ages of 60 and 70 and can cause rapid deterioration of memory and other cognitive functions, as well as behavioral changes, gait difficulties, involuntary movements, and visual problems. An accurate diagnosis is vital to rule out other treatable neurological pathologies that present similar symptoms, thus guiding the patient and their family.
Although CJD remains incurable and aggressive, and the search for alternatives is understandable, misinformation thrives in this context. The work with moringa compounds represents a scientific lead, not an immediate cure. The scenario has evolved from merely understanding the cause of the disease to testing ways to interfere with this process, which brings hope, provided it is accompanied by the scientific requirement for evidence.