Research teams from three institutions are using machine learning to predict how proteins associated with neurological diseases transform their shapes in microseconds.
Researchers from Google Research, the University of Milan, and the University of Cambridge; found out the shape transformations led to the death of brain cells.
Amyloid beta is the name of the key protein associated with implicating Alzheimer’s disease. This protein acquires a disordered shape within microseconds and reduces all its chances to stick back together. Therefore, forming toxic clusters that cause damage to the brain.
Developments from the research are likely to lead to future research that will help treat Parkinson’s disease and Alzheimer’s disease.
Both of which result from highly disordered proteins. A professor from the Cambridge Centre for Misfolding Diseases, Michele Vendruscolo, led the research and emphasized how medical research has researched how molecular proteins fold themselves into well-defined structures. However, the lead researcher claimed almost a third of the proteins do not fold. Instead, they adopt disordered shapes that most likely look like noodles.
In-motion Protein Molecules
Most approaches today focus on addressing the problem of disordered proteins as static structures and not those in motion. These approaches have posed a challenge in the treatment of protein-cause infections for the past 50 years. The problem is these proteins jump from one disordered shape to another within microseconds. However, the team coupled Google’s Computer network and generated massive amounts of short trajectories, which made it possible to define frequencies of shape transformation among the common motions. The researchers said the most common motions appear multiple times within the time frame.
Afterward, the researchers tallied the number of motions and predicted the state of occupation of the protein. They also established the time-frame within which a protein was able to transition. Nonetheless, the researchers focused their energy on the transition of the amyloid beta-peptide. These proteins are associated with causing Alzheimer’s disease, and the team believes their study will help future developments in the treatment of the disease.
The study will provide a strong basis for researching a variant of proteins that can move fast and in disordered motion—an area of study that has caused mystery among medical researchers for the past half a century.
