Researchers from Japan have discovered a way to stop the development of amyloid β fibers, which are associated with Alzheimer's disease, using an antibody that makes it possible to stop or delay the development of the fibers. This breakthrough may help develop new treatments for Alzheimer's disease
Researchers have identified a key mechanism in the development of Alzheimer's disease, which involves the growth and inhibition of amyloid β (Aβ) fibers. A recently discovered antibody is able to stop the development of fibers, thus offering a new approach to treatment that targets critical points in this growth.
A team of researchers from the Center for the Study of Life and Ecosystems, Institute of Molecular Science, and several universities in Japan—including Nagoya City University, Nagoya University, and Tsukuba University—unveiled a new mechanism behind the growth of amyloid β (Aβ) fibers, which are closely related to Alzheimer's disease. Using high speed atomic force microscopy (HS-AFM), they were able to observe in real time the growth of Aβ fibrils at the molecular level. This discovery provides new insight into how the fibers form and reveals possible ways to stop their progress.
Alzheimer's disease is a neurodegenerative disease that affects memory and cognitive function. One of its main drivers is the accumulation of Aβ proteins in the brain, which accumulate together and form fibers that interfere with normal brain function. Understanding the growth mechanism of these fibers and how to inhibit their formation is critical to the development of new treatments, but until now the specific mechanisms that led to their growth have been difficult to understand.
Alternating elongation and pausing of amyloid beta fibrils
The process of alternating elongation and retardation of amyloid β (Aβ) fibrils was documented by combining high-speed atomic force microscopy (HS-AFM) with Monte Carlo simulations. The study revealed the mechanism by which the 4396C antibody selectively binds to a "delayed" state of fiber growth, thereby preventing further elongation of Aβ fibers. Credit: The authors.
Insights into the mechanism of fiber growth
The researchers discovered that each Aβ fibril consists of two thin strands, called protofilaments. The protofilaments grow in an alternating pattern, with Aβ molecules added to each end of the strands one by one. A critical discovery in the study was that when the ends of the two protofilaments synchronize, the fiber enters a "suspended" state, where growth is temporarily stopped. This inhibition of growth is a key step in the process of Aβ fiber formation and may be the key to understanding the progression of Alzheimer's disease.
One of the most significant discoveries was the role of the antibody 4396C, which selectively binds to the ends of Aβ fibers in their suspended state. Once the antibody binds, the fiber is locked in this state and further growth is prevented. This discovery offers a promising new approach to stopping the growth of Aβ fibers and thereby slowing the progression of Alzheimer's disease.
Future implications and therapeutic predictions
The detailed observations made with HS-AFM allowed the research team to reveal the mechanism of alternating growth and retardation, which had not been detected before. By focusing on the delayed state of Aβ fibers, the research opens up new possibilities for developing treatments that may delay or stop Alzheimer's disease at the molecular level.
In the future, the team plans to investigate the action of the 4396C antibody in depth, with the hope of applying these findings to the development of new therapeutic approaches for Alzheimer's disease. In addition, the discovery may be relevant to other diseases related to protein accumulation, as the insights gained from the research may improve treatments for a variety of conditions that include protein accumulation.
More of the topic in Hayadan:
Comments
I thought the theory that acyloid plaques are the *cause* of Alzheimer's disease (and not a result of it) has long been disproved.
A. It has not been studied to work in human cells.
on. Even if it works it is not the final solution to Alzheimer's there are many other causes of the disease.
There is still a long way to go…