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Issue 12, 2016
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Square channels formed by a peptide derived from transthyretin

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Abstract

High-resolution structures of peptide supramolecular assemblies are key to understanding amyloid diseases and designing peptide-based materials. This paper explores the supramolecular assembly of a macrocyclic β-sheet peptide derived from transthyretin (TTR). The peptide mimics the β-hairpin formed by the β-strands G and H of TTR, which form the interface of the TTR tetramer. X-ray crystallography reveals that the peptide does not form a tetramer, but rather assembles to form square channels. The square channels are formed by extended networks of β-sheets and pack in a “tilted windows” pattern. This unexpected structure represents an emergent property of the peptide and broadens the scope of known supramolecular assemblies of β-sheets.

Graphical abstract: Square channels formed by a peptide derived from transthyretin

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Publication details

The article was received on 03 May 2016, accepted on 28 Jul 2016 and first published on 01 Aug 2016


Article type: Edge Article
DOI: 10.1039/C6SC01927G
Citation: Chem. Sci., 2016,7, 6946-6951
  • Open access: Creative Commons BY-NC license
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    Square channels formed by a peptide derived from transthyretin

    S. Yoo, A. G. Kreutzer, N. L. Truex and J. S. Nowick, Chem. Sci., 2016, 7, 6946
    DOI: 10.1039/C6SC01927G

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