5hpp

Publication Abstract from PubMed

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 beta-sheet peptide derived from transthyretin (TTR). The peptide mimics the beta-hairpin formed by the beta-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 beta-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 beta-sheets.

Square channels formed by a peptide derived from transthyretin.,Yoo S, Kreutzer AG, Truex NL, Nowick JS Chem Sci. 2016 Dec 1;7(12):6946-6951. doi: 10.1039/c6sc01927g. Epub 2016 Aug 1. PMID:28451128^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.