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Formation of toroids by self-assembly of an α–α corner mimetic: supramolecular cyclization

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Abstract

An α–α corner mimetic self-assembles to form a rod-like supramolecular structure which bends and closes end-to-end like a cyclization reaction to form uniform toroids. Each peptide fragment containing L-leucine, α-aminoisobutyric acid (Aib) and L-tyrosine forms rigid 310 helical structures stabilized by multiple intramolecular N–H⋯O hydrogen bonds. Two 310 helices are connected by the spacer 3-aminomethyl-benzylamine and maintain an angular distance of 120° and therefore mimic the α–α corner motif of a protein super secondary structure. The individual α–α corner subunits are themselves regularly interlinked through multiple water mediated intermolecular hydrogen-bonding interactions to form the rod-like supramolecular structure and toroids. The formation of the supramolecular structure has been proven with X-ray crystallography and other spectroscopic techniques. The cyclization of the supramolecular structure and toroid formation were studied by optical microscope, AFM and FE-SEM experiments. Despite other assignments such as exfoliation of graphene from graphite, the compound exhibits significant memory to finally produce the toroids.

Graphical abstract: Formation of toroids by self-assembly of an α–α corner mimetic: supramolecular cyclization

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Publication details

The article was received on 22 Jun 2017, accepted on 21 Aug 2017 and first published on 22 Aug 2017


Article type: Paper
DOI: 10.1039/C7TB01711A
Citation: J. Mater. Chem. B, 2017, Advance Article
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    Formation of toroids by self-assembly of an α–α corner mimetic: supramolecular cyclization

    D. Podder, S. Bera, M. Debnath, T. Das and D. Haldar, J. Mater. Chem. B, 2017, Advance Article , DOI: 10.1039/C7TB01711A

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