Self-folding of supramolecular polymers into bioinspired topology

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 approa...

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Bibliographic Details
Published in:Science advances 2018-09, Vol.4 (9), p.eaat8466-eaat8466
Main Authors: Prabhu, Deepak D, Aratsu, Keisuke, Kitamoto, Yuichi, Ouchi, Hayato, Ohba, Tomonori, Hollamby, Martin J, Shimizu, Nobutaka, Takagi, Hideaki, Haruki, Rie, Adachi, Shin-Ichi, Yagai, Shiki
Format: Article
Language:English
Subjects:
Biochemistry
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Summary: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.
ISSN:2375-2548
2375-2548
DOI:10.1126/sciadv.aat8466