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Nanoligomer Lead is Neuroprotective in Protein Misfolding Prion Disease: Findings published in ACS Chemical Neuroscience

Neuroinflammation, or inflammation in the brain, plays a significant role in many neurodegenerative diseases. These diseases, which include Alzheimer’s, Parkinson’s, and prion diseases, are all characterized by the buildup of misfolded proteins in the brain. As these proteins accumulate, they trigger chronic inflammation and damage the connections between neurons, leading to irreversible neuron death, cognitive decline, and eventually death. Unfortunately, there are currently very few treatments that can stop or slow the progression of these diseases. Sachi Bio recently published findings in ACS Chemical Neuroscience demonstrating neuroprotective effects of Nanoligomer lead in a model of Prion disease.


In this study, in collaboration with Sachi Bio, researchers at Colorado State University explored a new approach to directly target the inflammation in the brain by focusing on two specific molecules: NF-κB and NLRP3. These molecules are involved in triggering the inflammatory response in the brain. To test the effectiveness of this treatment, the researchers used a mouse model of prion disease, which mimics many features of neurodegenerative diseases, including the buildup of misfolded proteins, inflammation, neuron loss, and cognitive decline. They treated the prion-infected mice with NI112 either by injection or through the nose, aiming to see if it could reduce the symptoms and slow down disease progression. The results were promising: the treatment helped protect the mice from cognitive and behavioral problems associated with prion disease.


Additionally, the treatment significantly reduced inflammation in the brain by calming down the glial cells, which are responsible for triggering the immune response in the brain. It also prevented further loss of neurons and the development of spongy changes in the brain tissue, which are typical in prion diseases. Most importantly, the treated mice lived longer than those that did not receive the treatment, suggesting that this approach could extend life in cases of neurodegenerative diseases.


Prion diseases are a group of rare, but serious, brain disorders that affect both humans and animals. They are caused by abnormal proteins, called prions, that can misfold and spread in the brain. These misfolded prions cause damage to brain cells, leading to severe neurological problems and eventually death. What makes prion diseases particularly alarming is that they can spread from one person or animal to another through contaminated food, medical equipment, or even inherited genes in some cases.
In prion diseases, these abnormal proteins start to clump together in the brain, disrupting normal brain functions. This leads to symptoms such as memory loss, difficulty thinking, changes in behavior, and poor coordination. Over time, the damage becomes so severe that the brain begins to look "spongy" under a microscope due to the loss of brain cells, a condition called spongiform degeneration.

The findings provide strong evidence that targeting NF-κB and NLRP3 could be a promising strategy for treating neurodegenerative diseases like prion disease, Alzheimer’s, and Parkinson’s.


Because of the success in this prion disease model, the researchers plan to continue testing NI112 in other models of neurodegenerative diseases. If further studies show similar positive results, this treatment could eventually become a powerful tool in the fight against these devastating diseases.


Read more about this study:


Sydney J. Risen, Sean W. Boland, Sadhana Sharma, Grace M. Weisman, Payton M. Shirley, Amanda S. Latham, Arielle J. D. Hay, Vincenzo S. Gilberto, Amelia D. Hines, Stephen Brindley, Jared M. Brown, Stephanie McGrath, Anushree Chatterjee, Prashant Nagpal, and, Julie A. Moreno* (2024). ACS Chemical Neuroscience  15, 7, 1533-1547.

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