Scientists have discovered a method that may help prevent the formation of protein clumps associated with neurodegenerative diseases such as Alzheimer's, while simultaneously preserving the vital functions of these proteins within cells.
Protein droplets perform essential biological roles within cells, but in some pathological conditions, they can transform into solid masses known as protein fibers. This transformation disrupts their normal functions, including supporting microtubules that help transport substances within nerve cells.
In a study published in the journal Nature Communications, a research team of biophysicists at the University at Buffalo explained that a small molecule naturally found inside cells, known as L-arginine, can help stabilize protein droplets and prevent them from turning into harmful amyloid fibers.
The results show that this molecule helps maintain the liquid and functional state of protein droplets, and reduces the likelihood of pathological clumping, while preserving their ability to perform their normal functions within the cell.
The study indicates that the formation of protein droplets and the formation of disease-associated fibers are two separate processes, meaning that the cell may possess natural mechanisms that allow it to control these droplets and prevent them from turning into irreversible aggregates.
In this context, Dr. Priya R. Banerjee, a physics professor at the University at Buffalo and the lead author of the study, explained that the results suggest that cells may use small molecules such as arginine to keep these droplets stable and prevent them from turning into toxic forms.
She added that understanding this mechanism could open the door to developing new therapeutic molecules that target preventing the formation of protein fibrils associated with Alzheimer's disease and other neurological disorders.
Through an experimental model based on the tau protein, scientists discovered that fiber formation occurs on the surface of protein droplets and not inside them, suggesting that controlling this surface may be key to preventing pathological transformation.
One of the scientists on the team said that the inside of the droplet remains liquid and functional, while its surface forms the starting point for the formation of fibers, which opens the way for the possibility of preserving the droplets while preventing their deterioration.
These findings represent an important step in understanding the complex behavior of proteins within cells, and may contribute in the future to the development of therapeutic strategies targeting the early stages of neurodegenerative diseases.
