Researchers in the Gagné and Waters', in collaboration with the U.S. Army Research Office, published in the Journal of the American Chemical Society, report a functional synthetic model for studying the noncovalent networks, NCNs, required for complex protein functions.
The model -catenane is self-assembled from dipeptide building blocks and contains an extensive network of hydrogen bonds and aromatic interactions. Perturbations to the catenane cause compensating changes in the NCNs structure and dynamics, resulting in long-distance changes reminiscent of a protein.
Key findings include the notion that NCNs require regions of negative cooperativity, or "frustrated" noncovalent interactions, as a source of potential energy for driving the response. The Waters Group scientists refer to this potential energy as latent free energy and describe a mechanistic and energetic model for responsive systems. Teir work provides a conceptual basis for incorporating complex NCN-coupled functions in novel abiotic systems.