Tiny traps can provide new knowledge about difficult-to-treat diseases

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 shape to a more compact state so that proteins can pass in and out.
Illustration credit: Chalmers University of Technology | Julia Järlebark

Proteins that form clumps occur in many difficult-to-treat diseases, such as ALS, Alzheimer’s, and Parkinson’s. The mechanisms behind how the proteins interact with each other are difficult to study, but now researchers at Chalmers University of Technology, Sweden, have discovered a new method for capturing many proteins in nano-sized traps. Inside the traps, the proteins can be studied in a way that has not been possible before.

“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,” says Andreas Dahlin, professor at Chalmers, who led the research project.

Proteins that form clumps in our bodies cause a large number of diseases, including ALS, Alzheimer’s and Parkinson’s. A better understanding of how the clumps form could lead to effective ways to dissolve them at an early stage, or even prevent them from forming altogether. Today, there are various techniques for studying the later stages of the process, when the clumps have become large and formed long chains, but until now it has been difficult to follow the early development, when they are still very small. These new traps can now help to solve this problem.

Can study higher concentrations for longer time

The researchers describe their work as the world’s smallest gates that can be opened and closed at the touch of a button. The gates become traps, that lock the proteins inside chambers at the nanoscale. The proteins are prevented from escaping, extending the time they can be observed at this level from one millisecond to at least one hour. The new method also makes it possible to enclose several hundred proteins in a small volume, an important feature for further understanding.

“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,” says Andreas Dahlin.

In order for the technique to be used to study the course of specific diseases, continued development of the method is required.

“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,” says Andreas Dahlin.

How the new traps work

The gates that the researchers have developed consist of so-called polymer brushes positioned at the mouth of nano-sized chambers. The proteins to be studied are contained in a liquid solution and 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 start moving towards each other. In the traps, you can study individual clumps of proteins, which provides much more information compared to studying many clumps at the same time. For example, the clumps can be formed by different mechanisms, have different sizes and different structures. Such differences can only be observed if one analyses them one by one. In practice, the proteins can be retained in the traps for almost any length of time, but at present, the time is limited by how long the chemical marker – which they must be provided with to become visible – remains. In the study, the researchers managed to maintain visibility for up to an hour.

The research has been presented in the scientific article “Stable trapping of multiple proteins at physiological conditions using nanoscale chambers with macromolecular gates” recently published in Nature Communications.

The article is written by Justas Svirelis, Zeynep Adali, Gustav Emilsson, Jesper Medin, John Andersson, Radhika Vattikunta, Mats Hulander, Julia Järlebark, Krzysztof Kolman, Oliver Olsson, Yusuke Sakiyama, Roderick Y. H. Lim and Andreas Dahlin. The researchers are active at Chalmers University of Technology and the University of Basel.

Journal: Nature Communications
DOI: 10.1038/s41467-023-40889-4
Method of Research: Experimental study
Subject of Research: Not applicable
Article Title: Stable trapping of multiple proteins at physiological conditions using nanoscale chambers with macromolecular gates
Article Publication Date: 23-Aug-2023
COI Statement: The authors declare no competing interests.

Media Contact

Press Officer Emma Fry
Chalmers University of Technology
emma.fry@chalmers.se
Office: 031 772 50 28

Expert Contact

Professor Andreas Dahlin
Chalmers University of Technology
andreas.dahlin@chalmers.se
Cell: +46 31 772 28 44

www.chalmers.se

Media Contact

Press Officer Emma Fry
Chalmers University of Technology

All latest news from the category: Life Sciences and Chemistry

Articles and reports from the Life Sciences and chemistry area deal with applied and basic research into modern biology, chemistry and human medicine.

Valuable information can be found on a range of life sciences fields including bacteriology, biochemistry, bionics, bioinformatics, biophysics, biotechnology, genetics, geobotany, human biology, marine biology, microbiology, molecular biology, cellular biology, zoology, bioinorganic chemistry, microchemistry and environmental chemistry.

Back to home

Comments (0)

Write a comment

Newest articles

When the music changes, so does the dance

Controlling cooperative electronic states in Kagome metals. Playing a different sound track is, physically speaking, only a minute change of the vibration spectrum, yet its impact on a dance floor…

EcoFABs could lead to better bioenergy crops

Fabricated ecosystems created at Berkeley Lab will expedite microbiome research, and help underrepresented students in the classroom. A greater understanding of how plants and microbes work together to store vast…

Rice lab finds better way to handle hard-to-recycle material

Process transforms glass fiber-reinforced plastic into silicon carbide. Glass fiber-reinforced plastic (GFRP), a strong and durable composite material, is widely used in everything from aircraft parts to windmill blades. Yet…

Partners & Sponsors