Investigation of a Catenane with a Responsive Noncovalent Network: Mimicking Long-Range Responses in Proteins

We report a functional synthetic model for studying the noncovalent networks (NCNs) required for complex protein functions. The model [2]-catenane is self-assembled from dipeptide building blocks and contains an extensive network of hydrogen bonds and aromatic interactions. Perturbations to the cate...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2016-10, Vol.138 (40), p.13344-13352
Main Authors: Chung, Mee-Kyung, White, Peter S, Lee, Stephen J, Gagné, Michel R, Waters, Marcey L
Format: Article
Language:English
Subjects:
Anthracenes - chemistry
Biomimetic Materials - chemistry
Glycine - chemistry
Hydrogen Bonding
Models, Molecular
Molecular Conformation
Proteins - chemistry
Thermodynamics
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Summary:We report a functional synthetic model for studying the noncovalent networks (NCNs) required for complex protein functions. The model [2]-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. We refer to this potential energy as latent free energy and describe a mechanistic and energetic model for responsive systems.
ISSN:0002-7863
1520-5126
DOI:10.1021/jacs.6b07833