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Scientists at Durham University, working in partnership with Jagiellonian University in Poland, have developed a new nanoscale tool that can capture and precisely position some of the most important proteins in the human body, opening up new possibilities for medicine, imaging and bioengineering.
The research focuses on membrane proteins, which sit within the oily outer layer of cells and act as gatekeepers, controlling the movement of signals and materials into and out of the cell.
These proteins are essential for life and are the target of many modern medicines, yet they are notoriously difficult to study because of their fragile nature and complex structure.
To address this challenge, the team created tiny DNA “nano-rings” that can hold and organise individual membrane proteins with remarkable accuracy.
The approach combines two advanced techniques: DNA origami, which allows DNA to be folded into precise shapes, and nanodiscs, which are small, stable patches of membrane-like material that can carry single proteins.
By bringing these technologies together, the researchers developed what they call DNA-Origami-Constrained Nanodiscs, or DOC-NDs.
Professor Jonathan Heddle, one of the study’s lead researchers, said: “It’s an interesting example of how we can combine together different biological molecules, in this case, protein, DNA and lipids to make a sophisticated system that functions at the nanoscale.”
These structures, only tens of nanometres across, can trap protein-carrying nanodiscs inside a DNA ring while keeping the protein accessible for study.
Experiments showed that the system works efficiently, with most DNA rings successfully capturing nanodiscs and often holding just a single protein at a time.
This level of control is important for detailed scientific analysis and could improve imaging techniques such as cryo-electron microscopy, which relies on clear and consistent positioning of molecules.
The team also demonstrated an advanced version of the system that can control the orientation of individual proteins, meaning scientists can determine which way the protein is facing.
This is a significant step forward, as the orientation of membrane proteins is crucial to understanding how they function and how they interact with drugs.
Researchers say the platform could become a powerful new way to study membrane proteins and build more complex biological systems.
In the future, it may support the design of synthetic cells or enable the targeted delivery of proteins into specific membranes, offering far greater control than current methods.
The full study has been published in the journal Small Structures.
ENDS
Media Information
Professor Jonathan Heddle from Durham University is available for interview and can be contacted on jonathan.g.heddle@durham.ac.uk .
Alternatively, please contact Durham University Communications Office for interview requests on communications.team@durham.ac.uk or +44 (0)191 334 8623.
Source
‘Precise Capture of Membrane Proteins Using DNA-Origami-Constrained Nanodiscs’, (2026), J. Heddle et. al., Small Structures.
An embargoed copy of the paper is available from Durham University Communications Office. Please email Mr Araf Din, Communications Manager - communications.team@durham.ac.uk .
Graphics
Associated images are available via the following link: https://www.dropbox.com/scl/fo/jdjk6hfqqoabip6zbcvff/AH-Ew-A3nMn0uOJNvl6BcxE?rlkey=od526q4vgrx4uxbb69if6iiof&st=y8ib00rg&dl=0
Caption: Rendered in a retro-futuristic vapourwave style, the cover depicts DNA origami as luminous tweezers capturing membrane protein-loaded nanodiscs with nanometre precision. The image highlights DOC-NDs as a nanoscale tool for the controlled positioning of membrane proteins and their delivery to target lipid bilayers, shown as the planar surface where several proteins have already been delivered.
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