Issue 12, 2016

Square channels formed by a peptide derived from transthyretin

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

Supplementary files

Article information

Article type
Edge Article
Submitted
03 May 2016
Accepted
28 Jul 2016
First published
01 Aug 2016
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY-NC license

Chem. Sci., 2016,7, 6946-6951

Author version available

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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