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 10 degrees, which is done electrically. Then the polymers change their shap eto a more compact state so the proteins can pass in and out. Credit: Chalmers University of Technology | Julia Järlebark
Key points:
- Researchers developed a new method for capturing many proteins in nano-sized traps.
- The method uses traps or gates to cause hundreds of proteins to bump into each other and accumulate into clumps that can be studied for up to an hour.
- In the future, the method can be adapted to study the course of specific diseases that are caused by protein clumps, including ALS, Alzheimer’s, and Parkinson’s disease.
Proteins that form clumps in the body cause a number of diseases, including ALS, Alzheimer’s, and Parkinson’s disease. Understanding how clumps form could lead to effective methods to dissolve them or prevent them from forming, but studying the mechanisms underlying these protein interactions has been difficult.
Now, a study, published in Nature Communications, outlines a new method for capturing many proteins in nano-sized traps.
“We believe 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,” explained Andreas Dahlin, professor at Chalmers University of Technology.
Researchers developed traps or gates consisting of polymer brushes positioned at the mouth of nano-sized chambers. The proteins of interest, contained in a liquid solution, are attracted to the walls of the chambers after a special chemical treatment. When the gates are closed, the proteins can be freed from the walls and naturally bump into each other. As a result, the team could study clumps of hundreds of proteins.
Importantly, this method extends the amount of time protein clumps can be observed from one millisecond to at least one hour. A visibility of up to an hour allows researchers to study individual clumps of protein. As a result, they can examine different size and different structure clumps that form through distinct mechanisms.
Looking to the future, the team plans to develop the method so that it can be used to study the course of specific diseases.
“The traps need to be adapted to attract the proteins that are linked to the particular disease you are interested in,” said Dahlin. “What we’re working on now is planning which proteins are most suitable to study.”