ArticleAngewandte Chemie (International ed. in English)2017
A Two-Tailed Phosphopeptide Crystallizes to Form a Lamellar Structure.
Article in Angewandte Chemie (International ed. in English), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- Protein Design: From the Aspect of Water Solubility and Stability.Chemical reviews · 2022Review
- A Rapid Self-Assembly Peptide Hydrogel for Recruitment and Activation of Immune Cells.Molecules (Basel, Switzerland) · 2022Article
- Biomimetic peptide self-assembly for functional materials.Nature reviews. Chemistry · 2020Article
- Review
- Functional Coiled-Coil-like Assembly by Knob-into-Hole Packing of Single Heptad Repeat.ACS nano · 2019Article
- Hierarchically oriented organization in supramolecular peptide crystals.Protein and peptide letters · 2019Article
- Amphiphilic peptides as novel nanomaterials: design, self-assembly and application.International journal of nanomedicine · 2018Review
- A Two-Tailed Phosphopeptide Crystallizes to Form a Lamellar Structure.Angewandte Chemie (International ed. in English) · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 4 institutions in 3 countries.
Funding
Abstract
The crystal structure of a designed phospholipid-inspired amphiphilic phosphopeptide at 0.8 Å resolution is presented. The phosphorylated β-hairpin peptide crystallizes to form a lamellar structure that is stabilized by intra- and intermolecular hydrogen bonding, including an extended β-sheet structure, as well as aromatic interactions. This first reported crystal structure of a two-tailed peptidic bilayer reveals similarities in thickness to a typical phospholipid bilayer. However, water molecules interact with the phosphopeptide in the hydrophilic region of the lattice. Additionally, solid-state NMR was used to demonstrate correlation between the crystal structure and supramolecular nanostructures. The phosphopeptide was shown to self-assemble into semi-elliptical nanosheets, and solid-state NMR provides insight into the self-assembly mechanisms. This work brings a new dimension to the structural study of biomimetic amphiphilic peptides with determination of molecular organization at the atomic level.
Indexed as
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.