Evidence map›Paper›PMID 21488620›Full record

ArticleLangmuir : the ACS journal of surfaces and colloids2011

Effect of the peptide secondary structure on the peptide amphiphile supramolecular structure and interactions.

Dimitris Missirlis, Arkadiusz Chworos, Caroline J Fu, Htet A Khant, Daniel V Krogstad, Matthew Tirrell

Abstract read
In one paragraph

Article in Langmuir : the ACS journal of surfaces and colloids, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
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  4. Review
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  15. Fine-tuning the pH trigger of self-assembly.Journal of the American Chemical Society · 2012
    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

6 authors.

Dimitris MissirlisDepartment of Chemical Engineering, University of California, Santa Barbara, California 93106, United States. missirlis@uni-heidelberg.de
Arkadiusz Chworos
Caroline J Fu
Htet A Khant
Daniel V Krogstad
Matthew Tirrell

Funding

ZERNIKE PHASE PLATE CRYOEM IN OKAZAKIP41RR002250 · NCRR · UNIVERSITY OF ARIZONA · PI CHIU, WAH · 1985 to 2011
$22.1M
Tumor Therapy/Annihilation Using a Smart NanoPlatform (SNaP)U54CA119335 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ESENER, SADIK · 2005 to 2010
$21.2M
NCI NIH HHS 5 U54 CA119335-04NCI NIH HHS U54 CA119335NCRR NIH HHS P41 RR002250NCRR NIH HHS P41RR02250
6 · The paper itself

Abstract

Bottom-up fabrication of self-assembled nanomaterials requires control over forces and interactions between building blocks. We report here on the formation and architecture of supramolecular structures constructed from two different peptide amphiphiles. Inclusion of four alanines between a 16-mer peptide and a 16 carbon long aliphatic tail resulted in a secondary structure shift of the peptide headgroups from α helices to β sheets. A concomitant shift in self-assembled morphology from nanoribbons to core-shell worm-like micelles was observed by cryogenic transmission electron microscopy (cryo-TEM) and atomic force microscopy (AFM). In the presence of divalent magnesium ions, these a priori formed supramolecular structures interacted in distinct manners, highlighting the importance of peptide amphiphile design in self-assembly.

Indexed as

Hydrophobic and Hydrophilic InteractionsAmino Acid SequenceMagnesiumMolecular ImagingMolecular Sequence DataPeptidesProtein BindingProtein FoldingProtein Structure, SecondarySolutionsMagnesiumPeptidesSolutions

Identifiers

PMID21488620
PMCPMC3103120

What OpenQuestion holds

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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.