#Discovery #water #plays #essential #role #collagen #assembly
ENGINEERINGNET.BE – About a third of all proteins in the human body are collagen. It ensures the mechanical integrity of all human connective tissues.
Since collagen is formed in the aqueous environment of human cells, it makes sense that water plays a crucial role in its assembly.
Yet this connection has never been seriously investigated, according to Dr. Giulia Giubertoni of the Dutch University of Amsterdam. That is why she decided, together with her colleague Prof. Dr. Sander Woutersen and Prof. Dr. Gijsje Koenderink from TU Delft, to replace water with the heavier twin molecule D2O.
This molecule contains deuterium in place of the hydrogen atoms. The only difference is that deuterium has an extra neutron in its nucleus.
D2O is a natural replacement for regular water. But when interacting with proteins, D2O is less influential than H2O. This is because mutual bonds between D2O molecules are stronger than with H2O molecules. This weakens the interaction with proteins such as collagen.
Their research showed that the use of heavy water can accelerate collagen formation by up to ten times, leading to a less homogeneous, weaker and less stable network of collagen fibers.
The explanation is that with the reduced interaction with heavy water, it is easier for the collagen protein to shake off the D2O molecules and reorganize itself.
This accelerates the formation of the collagen network, but also results in a messier, suboptimal collagen network. Water thus acts as a kind of mediator between collagen molecules, slowing down their assembly and thus guaranteeing the functionality of living tissues.
This discovery offers opportunities for making new materials based on collagen. In addition, the macroscopic properties may be adjustable via subtle variations in the composition of the solvent, without making major changes to the chemical structure of the molecular building blocks.
Future research can also examine the role of water in the assembly of other proteins that also assemble into larger structures. Giubertoni will further study how defects in collagen proteins affect the interaction with water, and what role this plays in collagen diseases.
Partners in this research include the Max Planck Institute for Polymer Research in Germany and the Institute of Science and Technology Austria.
