08/09/2024
New paths for artificial nanofactories
Artificial nanofactories are tiny workshops made from the body's own molecules that are precisely designed and built according to a blueprint. In the future, they could help to better identify disease markers or environmental toxins, for example, or serve as highly specific catalysts for energy conversion and storage.
CENIDE member and researcher at the University of Duisburg-Essen, Prof. Dr. Barbara Saccà have developed a model that regulates the unfolding and degradation of proteins using compartmentalization strategies - which could pave the way for the development of artificial nanofactories. Their results have now been published in Nature Nanotechnology.
In cells, chemical reactions are organized in compartmentalized enzyme systems - that is, reactions take place in spatially limited areas, so-called compartments. This creates specific conditions for each reaction and improves the efficiency and control of biochemical processes.
Inspired by these natural systems, the research team at the University of Duisburg-Essen (UDE), led by CENIDE member Prof. Dr. Barbara Saccà from the Center for Medical Biotechnology (ZMB) in collaboration with the laboratory of Prof. Dr. Hemmo Meyer, has built an artificial structure that is divided into different compartments and mediates specific reactions. To do this, they use the DNA origami method - a technique in which DNA molecules are folded like tiny building blocks to form very small structures. "Since the interactions between the DNA components are precisely known, we can precisely design the structure into which the strand folds - down to the nanometer," explains the chemist.
In the UDE scientists' model, the artificial nanofactory consists of two such structures, each of which encloses a cavity. The protein folding machine p97, which - as its name suggests - unfolds proteins, is firmly anchored in the first part. In its now elongated form, the protein is then transported to the second area in a controlled manner. A protease is bound there, which breaks down the protein strand into small fragments. The spatial connection of the two sub-processes makes the reaction significantly more efficient: the reaction speed increases tenfold and undesired side reactions are reduced almost sixfold compared to two separate reactions, which are also not spatially separated.
"Our results show the potential of DNA nanotechnology for programming modular and compartmentalized enzyme systems and open up new avenues for synthetic biology and biocatalytic applications," says Saccà. In the future, the professor of bionanotechnology plans to further improve the origami factories: for example (1) by coating the origami with organic or inorganic materials that mimic the concept of a semi-permeable membrane or (2) by allowing access to the reaction chamber at only one point, thus better protecting the processes inside against external influences. "Advances of this kind could lead to the development of miniature laboratories with capabilities beyond those of natural systems."
Source: Center for Nanointegration Duisburg-Essen (CENIDE)