Evidence map›Paper›PMID 27936625›Full record

ArticleJournal of the American Chemical Society2016

Self-Assembly of an α-Helical Peptide into a Crystalline Two-Dimensional Nanoporous Framework.

Elizabeth L Magnotti, Spencer A Hughes, Rebecca S Dillard, Shengyuan Wang, Lillian Hough, Arshad Karumbamkandathil, Tianquan Lian, Joseph S Wall, Xiaobing Zuo, Elizabeth R Wright and 1 more

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed.

  1. Article
  2. 2D Assemblies Based on a Tetraphenylethylene D,L-Cyclic Peptide Scaffold.Angewandte Chemie (International ed. in English) · 2025
    Article
  3. Article
  4. Exo-chirality of the α-helix.Nature communications · 2024
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Protein Assembly by Design.Chemical reviews · 2021
    Review
  13. Article
  14. Review
  15. Review
  16. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors.

Elizabeth L MagnottiDepartment of Chemistry, Emory University , Atlanta, Georgia 30322, United States.
Spencer A HughesDepartment of Chemistry, Emory University , Atlanta, Georgia 30322, United States.
Rebecca S DillardDepartment of Pediatrics, Emory University School of Medicine, Children's Healthcare of Atlanta , Atlanta, Georgia 30322, United States.
Shengyuan WangDepartment of Chemistry, Emory University , Atlanta, Georgia 30322, United States.
Lillian HoughDepartment of Chemistry, Emory University , Atlanta, Georgia 30322, United States.
Arshad KarumbamkandathilDepartment of Chemistry, Emory University , Atlanta, Georgia 30322, United States.
Tianquan LianDepartment of Chemistry, Emory University , Atlanta, Georgia 30322, United States.ORCID 0000-0002-8351-3690
Joseph S WallBrookhaven National Laboratory , P.O. Box 5000, Upton, New York 11973, United States.
Xiaobing ZuoX-ray Science Division, Argonne National Laboratory , 9700 South Cass Avenue, Argonne, Illinois 60439, United States.
Elizabeth R WrightDepartment of Pediatrics, Emory University School of Medicine, Children's Healthcare of Atlanta , Atlanta, Georgia 30322, United States.
Vincent P ConticelloDepartment of Chemistry, Emory University , Atlanta, Georgia 30322, United States.

Funding

Virology and Molecular Biomarkers CoreP30AI050409 · NIAID · EMORY UNIVERSITY · PI Carlos del Rio · 2002 to 2026
$74.0M
Atlanta Clinical and Translational Science Institute (ACTSI) RenewalUL1TR000454 · NCATS · EMORY UNIVERSITY · PI STEPHENS, DAVID S · 2012 to 2016
$25.8M
Structure and Function of Prokaryotic Appendages by Cryo-Electron TomographyR01GM104540 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI WRIGHT, ELIZABETH R · 2013 to 2017
$1.4M
FEI Transmission Electron Microscope with Tomography CapabilityS10RR025679 · NCRR · EMORY UNIVERSITY · PI SPEARMAN, PAUL W. · 2009 to 2009
$500k
NCATS NIH HHS UL1 TR000454NCRR NIH HHS S10 RR025679NIAID NIH HHS P30 AI050409NIGMS NIH HHS R01 GM104540
6 · The paper itself

Abstract

Sequence-specific peptides have been demonstrated to self-assemble into structurally defined nanoscale objects including nanofibers, nanotubes, and nanosheets. The latter structures display significant promise for the construction of hybrid materials for functional devices due to their extended planar geometry. Realization of this objective necessitates the ability to control the structural features of the resultant assemblies through the peptide sequence. The design of a amphiphilic peptide, 3FD-IL, is described that comprises two repeats of a canonical 18 amino acid sequence associated with straight α-helical structures. Peptide 3FD-IL displays 3-fold screw symmetry in a helical conformation and self-assembles into nanosheets based on hexagonal packing of helices. Biophysical evidence from TEM, cryo-TEM, SAXS, AFM, and STEM measurements on the 3FD-IL nanosheets support a structural model based on a honeycomb lattice, in which the length of the peptide determines the thickness of the nanosheet and the packing of helices defines the presence of nanoscale channels that permeate the sheet. The honeycomb structure can be rationalized on the basis of geometrical packing frustration in which the channels occupy defect sites that define a periodic superlattice. The resultant 2D materials may have potential as materials for nanoscale transport and controlled release applications.

Indexed as

NanoporesModels, MolecularPeptidesProtein Conformation, alpha-HelicalPeptides

Identifiers

PMID27936625
PMCPMC5739522

What OpenQuestion holds

Textmetadata
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Read underepoch 390

Registered trials

None linked

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.