The image shows the protein traps, which consist of nanoscale chambers and polymers that form gates above. These “doors” are opened up by increasing the temperature by about ten degrees, which is done electrically. Then the polymers change their shape to a more compact state so that proteins can pass in and out. Credit: Chalmers University of Technology | Julia Järlebark
Researchers from Chalmers University of Technology in Sweden have developed a novel method for capturing proteins in nano-sized traps, allowing them to be studied in ways that previously were not possible. The protein traps developed will aid researchers in studying difficult-to-treat diseases such as ALS, Alzheimer’s, and Parkinson's.
In diseases such as Alzheimer’s proteins often form clumps and the mechanisms behind their interaction have been difficult to study. With methods presented by the researchers, these proteins can be studied in greater detail than previously thought. "We believe that our method has great potential to increase the understanding of early and dangerous processes in a number of different diseases and eventually lead to knowledge about how drugs can counteract them," said Andreas Dahlin a professor at Chalmers.
The research, published in Nature Communications, outlines the functionality of the protein traps.
The traps contain gates made up of polymer brushes that can be opened or closed with the push of a button. Once closed the proteins are trapped inside, allowing researchers to study large concentrations of these proteins for an extended amount of time.
"The clumps that we want to see and understand better consist of hundreds of proteins, so if we are to study them, we need to be able to trap such large quantities. The high concentration in the small volume means that the proteins naturally bump into each other, which is a major advantage of our new method," said Andreas Dahlin.
The next steps for the traps include optimizing them to increase selectivity for specific proteins related to diseases. "The traps need to be adapted to attract the proteins that are linked to the particular disease you are interested in. What we're working on now is planning which proteins are most suitable to study," said Dahlin.