Many protein functions show complex structural or dynamic changes in response to a stimulus, for instance, allostery, binding through induced fit, conformational selection, signal transduction, etc. However, there are very few synthetic systems showing these complex responses since the small molecule models generally rely on one or two dominant interactions instead of a network of interactions.<br/><br/>Herein, we report two synthetic models of intermediate complexity generated from the dynamic covalent chemistry approach and their biomimetic responses to stimuli. One type is a set of tetrameric pseudo-peptide receptors for protonated cytidines. The study of their binding properties discloses that they can bind more than one guest, and that the binding of the first guest significant impacts the kinetics of binding a second guest, recapitulating the complex properties of both induced fit binding and allostery in proteins. The other type is a set of [2]-catenanes self-assembled from dipeptide building blocks, containing an extensive network of hydrogen bonds and aromatic interactions. The perturbation study offers the molecular level response of a catenane noncovalent interaction network to a mutation-induced stress, resulting in long-distance changes reminiscent of signal transduction in a protein. These biomimetic responses of both systems to stimuli will be addressed in detail.<br/>

Tetrameric pseudo-peptide receptors with allosteric properties and [2]-catenanes with a responsive noncovalent network mimicking long-range responses in proteins

254th National Meeting (2017)

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