Download MendeleySquare channels formed by a peptide derived from transthyretin.
Yoo, S., Kreutzer, A.G., Truex, N.L., Nowick, J.S.(2016) Chem Sci 7: 6946-6951
- PubMed: 28451128
- DOI: https://doi.org/10.1039/c6sc01927g
- Primary Citation of Related Structures:
5HPP - PubMed 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.
Organizational Affiliation:
Department of Chemistry , University of California , Irvine , California 92697-2025 , USA . Email: jsnowick@uci.edu.
