ArticleChemical science2016
Square channels formed by a peptide derived from transthyretin.
Article in Chemical science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Crystallization and 1.6 Å resolution crystal structure of an acylated GLP-1/GIP analogue peptide.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Dissecting the Conformational Stability of a Glycan Hairpin.Journal of the American Chemical Society · 2024Article
- Assembly of π-Stacking Helical Peptides into a Porous and Multivariable Proteomimetic Framework.Journal of the American Chemical Society · 2022Article
- Synthesis and study of macrocyclic β-hairpin peptides for investigating amyloid oligomers.Methods in enzymology · 2021Article
- Interpenetrating Cubes in the X-ray Crystallographic Structure of a Peptide Derived from MedinJournal of the American Chemical Society · 2020Article
- A Tetramer Derived from Islet Amyloid Polypeptide.The Journal of organic chemistry · 2017Article
- Crystal Structure of the DFNKF Segment of Human Calcitonin Unveils Aromatic Interactions between Phenylalanines.Chemistry (Weinheim an der Bergstrasse, Germany) · 2017Article
- Stabilization, Assembly, and Toxicity of Trimers Derived from Aβ.Journal of the American Chemical Society · 2017Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.