by A groundbreaking study, recently published in Nature Communications, sheds light on the formation of protein clumps in Alzheimer’s disease. Led by researchers from Karolinska Institutet, this study offers new insights into the underlying mechanisms and could pave the way for innovative treatments for this devastating neurodegenerative disorder.
Alzheimer’s disease, affecting millions of people worldwide, is characterized by symptoms such as memory loss, confusion, and cognitive decline. One of the main hallmarks of the disease is the accumulation of abnormal protein clumps, known as amyloid fibrils and plaques, in the brain. These clumps disrupt the normal functioning of brain cells and may trigger inflammation and cell death.
Scientists have long sought to understand the formation of these fibrils and find ways to prevent their formation. One approach involves using proteins called molecular chaperones, which can bind to specific sites on the surface of the fibrils and inhibit the generation of new aggregates. Molecular chaperones are naturally present in cells and assist in the proper folding and functioning of other proteins.
In this study, the researchers focused on a specific molecular chaperone called BRICHOS. Previous research has shown that BRICHOS can inhibit the formation of amyloid fibrils. The goal was to uncover how BRICHOS recognizes and attaches to the fibril surface, providing insights into the regions where new aggregates are produced. The team at the Laboratory for Protein Misfolding and Assembly, Department of Biosciences and Nutrition, Karolinska Institutet, employed advanced structural biology techniques, including solid-state nuclear magnetic resonance (NMR) and electron microscopy, to visualize the interactions between BRICHOS and the fibrils at an atomic level.
Their findings revealed that BRICHOS can detect and bind to specific regions, known as aggregation hotspots, on the fibrils. By binding to these hotspots, BRICHOS likely prevents the formation of further aggregates, thereby suppressing their toxic effects.
Targeting these aggregation hotspots could be a promising avenue for interfering with the fibril formation process and mitigating the harmful effects of Alzheimer’s disease. The researchers also intend to investigate whether similar mechanisms are at play in other neurodegenerative disorders, such as Parkinson’s disease, which also involve protein aggregation.
Notably, this study was conducted in collaboration with research groups in Lyon, France, and Riga, Latvia. These partnerships provided access to new solid-state NMR instrumentation and additional expertise.
The findings of this study offer hope for the development of innovative treatments for Alzheimer’s disease. By understanding how protein clumps form and identifying ways to disrupt their formation, researchers are getting closer to finding a solution for this devastating disorder.
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1. Source: Coherent Market Insights, Public sources, Desk research
2. We have leveraged AI tools to mine information and compile it
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