How DNA Origami Manipulates Proteins For Bioengineering
Physical manipulation of microscopic structures and proteins allows scientists to alter cell biology.
For most, this small scale approach provides a vital link between natural responses in cells and medical intervention. This approach could open up new opportunities in cell biology, biotechnology, and medication.
At the heart of this is DNA origami. This recent technique in the creation of hybrid structures takes DNA and proteins to form new, more beneficial components. It is the work of Florian Praetorius and Prof. Hendrik Dietz of the Technical University of Munich and is sure to replicate elsewhere.
What is DNA origami and why is this such an important breakthrough?
DNA Origami is the non-scientific term for the act of folding and manipulating proteins and DNA strands.
Researchers take these elements and reconstruct them into whole new structures. This means that scientists can now reassemble and create new biological building blocks. They are not folding a material to make something intricate and beautiful, like making a crane from paper.
These elements are still beautiful in their way, but this is not the main aim here. Instead, they are folding it to make something functional on a molecular level. This is important in biotechnological fields.
There were once limitations in the creation of structures via chemical synthesis. No construction could take place within a biological environment, until now at least.
This folding and “origami” technique is primarily the result of natural “staples.”
Instead of manipulating these shapes in an invasive manner, this new folding method creates shapes inside cells through genetic encoding. It is all about taking two parts of the DNA strand and connecting them together to create that fold, rather than the fold itself. The designers talk about “stapling.”
This is perhaps a bit of a misleading way to say the physical process, yet still a more right term for this biological bind.
What happens here is that researchers bring in synthetic variants of bacteria – known as TAL proteins. These proteins are naturally active components that will target areas of interest in the DNA strand and join them together.
TAL proteins manipulated through engineering target specific areas to form those intricate shapes.
The added benefit here is that these proteins carry out the work inside the cell. This means it all occurs after any chemical synthesis and protein production takes place.
A lack of chemical synthesis also means minimal human interaction beyond the initial genetic programming. The elements come from the cells and are autonomously assembled. This opens doors for molecular manipulation within cells and new structure designs.
This binding and stapling are then utilized in such a way that they create diverse, complex new structures.
One binding site and staple provides one form of protein reformation for one new purpose. Researchers do not have to stop at one site or one form of protein per structure.
With the folding method perfected, researchers can use it in many ways. The more binding sites that there are in these cells, the more opportunities there are to manipulate the structure and create new ones.
On top of this, these “staple” proteins can also act as anchors, where any strands can become attached. This genetic fusion can allow for extra proteins to attach to the DNA – either other DNA strands or other helpful components. This further complicates the design and allows for a more diverse range of new structures.
Why is this all so important in genetic research and biomechanics?
DNA origami is not simple a neat trick that lets scientists play with shapes and create beautiful microscopic images. While the folded mass of proteins is attractive on its way, there is a possible element here.
Hopefully, this new technique could alter the way that we read the genetic code and process genetic information. Genes could be then hidden or exposed, depending on their worth or detriment to the cell.
The use of protein manipulation could help to stimulate immune response in cells. This would create new opportunities in aiding auto-immune issues and disease prevention.
Furthermore, there is the chance that it could improve biotechnological processes. It seems that this folding technique could have plenty of untapped potentials.