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A KAIST-led research team has found that a protein involved in gene regulation can suppress the harmful aggregation of amyloid-beta, a peptide associated with Alzheimer's disease. The approach also reduced the toxicity of protein aggregates that had already formed.

In experiments using a mouse model of Alzheimer's disease, the treatment reduced protein accumulation in the brain and improved memory recognition, suggesting a possible route toward new therapeutics.

The research team led by Professor Mi Hee Lim from the Department of Chemistry identified a new approach to controlling the aggregation and toxicity of amyloid-beta. The findings were published in Advanced Science.

The study was conducted in collaboration with Professor Seung Jae Lee's team in the Department of Chemistry at Jeonbuk National University, Dr. Chul-Ho Lee and Dr. Kyoung-Shim Kim of the Korea Research Institute of Bioscience and Biotechnology (KRIBB), Dr. Young-Ho Lee of the Korea Basic Science Institute (KBSI), and Dr. Jiyong Park of the Institute for Basic Science (IBS).

One of the hallmarks of Alzheimer's disease is the abnormal aggregation and accumulation of amyloid-beta in the brain. Toxic aggregates formed during this process can damage nerve cells. The team sought to suppress this harmful aggregation and reduce the toxicity of existing aggregates.

The team used a zinc finger protein, which is best known for its role in gene regulation. Zinc ions stabilize the protein's folded structure, enabling it to recognize DNA or RNA.

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