Study Of Disordered Protein Hopping Open Doors For Future Alzheimer's Disease Therapies

The University of Cambridge, the University of Milan, and Google Research engineers have used machine learning tools to predict the role of proteins, especiallythe onesconcernedwith neurological diseases, in changing their shapes within microseconds. The proteins named amyloid beta that exist in the Alzheimer's disease are found to avoid sticking together or forming any toxic clusters by bringing about an extreme alterations in their shape. With the help of the current study published in the journal Nature Computational Science, the researchers hope to create new treatments for diseases occurring due to disordered proteins, such as Parkinson's disease, Alzheimer's disease, and so on.

The researchers define proteins as molecules that can be folded into well-defined structures but the process of how it occurs is being researched on from the past few decades. According to Professor Michele Vendruscolo from Cambridge, majority of the proteins in our body do not fold and tend to remain disordered. The current focus is to work toward gathering more knowledge over the behavior of these disordered proteins as the earlier methods addressed only static structures and not structures in motion. The latest approach used Google's computer network to create large copies of short trajectories. The computer helped study the motions and find the number of times disordered proteins jumps between dissimilar shapes.

The motion study sheds more light on the state the protein occupies and its transition phase as well. The amyloid beta peptide — which is a protein fragment found in Alzheimer's disease — was scrutinized by the researchers as this protein was found to form plaques in the brains of Alzheimer's patient. They also found the protein to jump between different states a million times per second because of which the drugging of amyloid beta still remains impossible. However, study on the variant of amyloid beta has helped researchers toresistant the aggregation. They found the oxidated amyloid beta to change shape thereby explaining that the decrease in aggregation is possible through either making it more disordered. The self-associating in aberrant manners could thus be prevented bymaking proteins even more disordered.