Square channels formed by a peptide derived from transthyretin.

نویسندگان

  • Stan Yoo
  • Adam G Kreutzer
  • Nicholas L Truex
  • James S Nowick
چکیده

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.

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عنوان ژورنال:
  • Chemical science

دوره 7 12  شماره 

صفحات  -

تاریخ انتشار 2016