An illustration depicts nano traps, designed as nanoscale chambers with polymer-based gates above them. By electrically increasing the temperature approximately 10 degrees, these gates open, allowing the polymers to shift into a more compact form. This change permits proteins to move in and out. The image is credited to Chalmers University of Technology and captured by Julia Järlebark.
Protein aggregates play a crucial role in numerous difficult diseases, including ALS, Alzheimer’s, and Parkinson’s. Grasping how these proteins interact is a complex task. Yet, the team at Chalmers University of Technology in Sweden has pioneered a method to capture a multitude of proteins within tiny nano traps. This breakthrough offers novel insights into protein dynamics.
“Our technique holds immense promise in enhancing our comprehension of early and perilous stages in various diseases and could eventually inform drug development strategies to counter these conditions,” remarks Andreas Dahlin, the leading professor from Chalmers who spearheaded this study.
The clumping of proteins is a key factor in diseases like ALS, Alzheimer’s, and Parkinson’s. Gaining an in-depth understanding of these clumps’ formation could pave the way for effective early-stage dissolution strategies, or potentially prevent their formation.
Andreas Dahlin, Professor in the Department of Chemistry and Chemical Engineering at Chalmers University of Technology, is credited for this work. The image credit goes to Chalmers University of Technology and photographer Mikael Terfors.
Currently, there are various techniques to study the later stages of clumping when the aggregates have grown into longer chains. However, monitoring the initial stages, when they are small, has been challenging. The new nano traps now offer a solution to this issue.
Extended Study Time at Higher Concentrations
The team describes their innovation as the world’s tiniest gates, operable at the press of a button. These gates serve as traps, confining proteins within nanoscale chambers. This setup significantly prolongs the observation period of proteins at this scale, from a mere millisecond to over an hour. Moreover, the method enables the confinement of hundreds of proteins within a small space, which is crucial for deeper understanding.
“We aim to observe and better comprehend clumps comprising hundreds of proteins. To study such large quantities, our method’s ability to trap them in high concentrations within a small area is invaluable. This high concentration facilitates natural collisions among proteins, a key advantage of our technique,” explains Andreas Dahlin.
For the method to be applicable in specific disease studies, further development is essential.
“Our current focus is to tailor the traps to target proteins associated with specific diseases. We are strategizing on the most appropriate proteins for our studies,” Dahlin adds.
Understanding the New Traps
The devised gates consist of polymer brushes at the entrances of nanoscale chambers. The proteins, suspended in a liquid solution, are drawn to the chamber walls after special chemical treatment.
Once the gates close, proteins detach from the walls and start clustering. These traps enable the study of individual protein clumps, offering more detailed information than observing multiple clumps simultaneously. Variations in formation mechanisms, sizes, and structures of clumps can only be discerned through individual analyses. Currently, proteins can be held in the traps for extensive periods, limited only by the lifespan of the chemical markers used for visibility. In this research, visibility was maintained for up to an hour.
The study, titled “Stable trapping of multiple proteins at physiological conditions using nanoscale chambers with macromolecular gates” by Justas Svirelis, Zeynep Adali, and others, was published on 23 August 2023 in Nature Communications. The DOI is 10.1038/s41467-023-40889-4.
Funding for the study came from the European Research Council and the Erling-Persson Family Foundation.
Frequently Asked Questions (FAQs) about Nano Traps Research
What are the nano traps developed at Chalmers University of Technology?
Nano traps are nanoscale chambers with polymer-based gates, designed by researchers at Chalmers University of Technology. They can trap proteins by opening and closing the gates through temperature changes, allowing for detailed study of protein behaviors implicated in diseases like ALS, Alzheimer’s, and Parkinson’s.
How do the nano traps help in understanding protein clumps in diseases?
The nano traps allow for the capture and extended observation of proteins at a nanoscale level. This aids in studying the early development of protein clumps, which is crucial for understanding diseases like ALS, Alzheimer’s, and Parkinson’s, and could lead to new treatment strategies.
Who led the research project on nano traps at Chalmers University?
Professor Andreas Dahlin, from the Department of Chemistry and Chemical Engineering, led the research project on nano traps at Chalmers University of Technology.
What is the significance of the new method developed for studying protein clumps?
The new method using nano traps represents a significant advancement in studying the early stages of protein clumping. It allows for the observation of proteins at higher concentrations and for longer periods, providing insights that were previously difficult to obtain.
How do the nano traps function?
The nano traps function by using polymer brushes as gates at the mouth of nanoscale chambers. When the temperature is increased electrically, these gates open, allowing proteins in a liquid solution to enter the chambers. Once inside, the proteins can be studied individually, providing detailed insights into their behavior and clumping processes.
More about Nano Traps Research
- Chalmers University of Technology Official Website
- Nature Communications Journal
- Research on Protein Clumps in Neurodegenerative Diseases
- Profile of Professor Andreas Dahlin
- European Research Council Funding Information
- Erling-Persson Family Foundation