Evidence map›Paper›PMID 25144245›Full record

ArticleJournal of the American Chemical Society2014

Amino acid sequence in constitutionally isomeric tetrapeptide amphiphiles dictates architecture of one-dimensional nanostructures.

Honggang Cui, Andrew G Cheetham, E Thomas Pashuck, Samuel I Stupp

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
12.4field-weighted citation impact, top 1% of its field
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

78 citing papers in PubMed, 298 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
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  8. ATP-Regulated Formation of Transient Peptide Amphiphiles Superstructures.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Assessment of the MARTINI 3 Performance for Short Peptide Self-Assembly.Journal of chemical theory and computation · 2024
    Article
  16. Discovery, validation, and prodrug design of an ACE2 activator for treating bacterial infection-induced lung inflammation.Journal of controlled release : official journal of the Controlled Release Society · 2023
    Article
  17. Article
  18. Review
  19. Article
  20. Article

18 more citing papers are in PubMed but not listed here.

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

4 authors at 2 institutions in 1 country.

Honggang CuiDepartment of Materials Science and Engineering, ‡Department of Chemistry, §Department of Medicine, and ⊥Department of Biomedical Engineering, Northwestern University , 2220 Campus Drive, Evanston, Illinois 60208, United States.
Andrew G Cheetham
E Thomas Pashuck
Samuel I Stupp
Northwestern University · USJohns Hopkins University · US

Funding

X-RAY STUDY OF HORMONE-RECEPTOR AND PROTEIN-ANTIBODY COMPLEXESP41RR007707 · NCRR · UNIVERSITY OF CHICAGO · PI YANG, XIANGZHONG · 2002 to 2011
$17.3M
BioCARS: A Synchrotron Structure Biology ResourceR24GM111072 · NIGMS · UNIVERSITY OF CHICAGO · PI MOFFAT, JOHN KEITH · 2013 to 2016
$2.3M
NCRR NIH HHS P41 RR007707NCRR NIH HHS RR007707
6 · The paper itself

Abstract

The switching of two adjacent amino acids can lead to differences in how proteins fold thus affecting their function. This effect has not been extensively explored in synthetic peptides in the context of supramolecular self-assembly. Toward this end, we report here the use of isomeric peptide amphiphiles as molecular building blocks to create one-dimensional (1D) nanostructures. We show that four peptide amphiphile isomers, with identical composition but a different sequence of their four amino acids, can form drastically different types of 1D nanostructures under the same conditions. We found that molecules with a peptide sequence of alternating hydrophobic and hydrophilic amino acids such as VEVE and EVEV self-assemble into flat nanostructures that can be either helical or twisted. On the other hand, nonalternating isomers such as VVEE and EEVV result in the formation of cylindrical nanofibers. Furthermore, we also found that when the glutamic acid is adjacent to the alkyl tail the supramolecular assemblies appear to be internally flexible compared to those with valine as the first amino acid. These results clearly demonstrate the significance of peptide side chain interactions in determining the architectures of supramolecular assemblies.

Indexed as

Amino Acid SequenceNanofibersNanostructuresOligopeptidesProtein Structure, SecondaryX-Ray DiffractionOligopeptides

Identifiers

PMID25144245
PMCPMC4156871
OpenAlexW2328665600

What OpenQuestion holds

Textmetadata
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.