Self-folding of supramolecular polymers into bioinspired topology.

Prabhu, DD; Aratsu, K; Kitamoto, Y; Ouchi, H; Ohba, T; Hollamby, MJ; Shimizu, N; Takagi, H; Haruki, R; Adachi, S-I; Yagai, S

Abstract

Folding one-dimensional polymer chains into well-defined topologies represents an important organization process for proteins, but replicating this process for supramolecular polymers remains a challenging task. We report supramolecular polymers that can fold into protein-like topologies. Our approach is based on curvature-forming supramolecular rosettes, which affords kinetic control over the extent of helical folding in the resulting supramolecular fibers by changing the cooling rate for polymerization. When using a slow cooling rate, we obtained misfolded fibers containing a minor amount of helical domains that folded on a time scale of days into unique topologies reminiscent of the protein tertiary structures. Thermodynamic analysis of fibers with varying degrees of folding revealed that the folding is accompanied by a large enthalpic gain. The self-folding proceeds via ordering of misfolded domains in the main chain using helical domains as templates, as fully misfolded fibers prepared by a fast cooling rate do not self-fold.

Citation

Prabhu, D., Aratsu, K., Kitamoto, Y., Ouchi, H., Ohba, T., Hollamby, M., …Yagai, S. (2018). Self-folding of supramolecular polymers into bioinspired topology. Science Advances, 4(9), Article eaat8466. https://doi.org/10.1126/sciadv.aat8466

• Journal Article Type: Article
• Acceptance Date: Jul 27, 2018
• Publication Date: Sep 7, 2018
• Journal: Science Advances
• Publisher: American Association for the Advancement of Science
• Peer Reviewed: Peer Reviewed
• Volume: 4
• Issue: 9
• Article Number: eaat8466
• DOI: https://doi.org/10.1126/sciadv.aat8466
• Publisher URL: http://doi.org/10.1126/sciadv.aat8466