Evidence map›Paper›PMID 24085660›Full record

ArticleThe European physical journal. E, Soft matter2013

Self-assembly and gelation properties of glycine/leucine Fmoc-dipeptides.

Claire Tang, Rein V Ulijn, Alberto Saiani

Open access · hybridAbstract read
PubMed Publisher
In one paragraph

Article in The European physical journal. E, Soft matter, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
3.6field-weighted citation impact, top 8% 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

5 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Stable Formulations of Peptide-Based Nanogels.Molecules (Basel, Switzerland) · 2020
    Article
  5. Review
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

3 authors at 2 institutions in 1 country.

Claire TangSchool of Materials, The University of Manchester, Grosvenor Street, M1 7HS, Manchester, UK.
Rein V Ulijn
Alberto Saiani
University of Manchester · GBUniversity of Strathclyde · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Self-assembly of aromatic peptide amphiphiles is known to be driven by a combination of π-π stacking of the aromatic moieties and hydrogen bonding between the peptide backbones, with possible stabilisation from the amino acid side chains. Phenylalanine-based Fmoc-dipeptides have previously been reported for their characteristic apparent pKa transitions, which were shown to coincide with significant structural and morphological changes that were peptide sequence dependent. Here, phenylalanine was replaced by leucine and the effect on the self-assembling behaviour of Fmoc-dipeptides was measured using potentiometry, fluorescence and infrared spectroscopy, transmission electron microscopy, X-ray scattering and shear rheometry. This study provides additional cues towards the elucidation of the sequence-structure relationship in self-assembling aromatic peptide amphiphiles.

Indexed as

DipeptidesGelsDipeptidesFmoc-Leu-Gly-OHGels

Identifiers

PMID24085660
OpenAlexW2048799253

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.