Evidence map›Paper›PMID 29498711›Full record

ArticleMolecules (Basel, Switzerland)2018

Search for Fibrous Aggregates Potentially Useful in Regenerative Medicine Formed under Physiological Conditions by Self-Assembling Short Peptides Containing Two Identical Aromatic Amino Acid Residues.

Justyna Fraczyk, Wojciech Lipinski, Agata Chaberska, Joanna Wasko, Kamil Rozniakowski, Zbigniew J Kaminski, Maciej Bogun, Zbigniew Draczynski, Elzbieta Menaszek, Ewa Stodolak-Zych and 2 more

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
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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

12 authors.

Justyna FraczykInstitute of Organic Chemistry, Lodz University of Technology, Zeromskiego 116, 90-924 Lodz, Poland. justyna.fraczyk@p.lodz.pl.
Wojciech LipinskiInstitute of Organic Chemistry, Lodz University of Technology, Zeromskiego 116, 90-924 Lodz, Poland. wojtek.p.lipinski@gmail.com.
Agata ChaberskaInstitute of Organic Chemistry, Lodz University of Technology, Zeromskiego 116, 90-924 Lodz, Poland. agata.chaberska@p.lodz.pl.
Joanna WaskoInstitute of Organic Chemistry, Lodz University of Technology, Zeromskiego 116, 90-924 Lodz, Poland. joanna.wasko@p.lodz.pl.
Kamil RozniakowskiInstitute of Organic Chemistry, Lodz University of Technology, Zeromskiego 116, 90-924 Lodz, Poland. kamilrozniakowski@wp.pl.
Zbigniew J KaminskiInstitute of Organic Chemistry, Lodz University of Technology, Zeromskiego 116, 90-924 Lodz, Poland. zbigniew.kaminski@p.lodz.pl.
Maciej BogunDepartment of Material and Commodity Sciences and Textile Metrology, Lodz University of Technology, Zeromskiego 116, 90-924 Lodz, Poland. maciej.bogun@p.lodz.pl.
Zbigniew DraczynskiDepartment of Material and Commodity Sciences and Textile Metrology, Lodz University of Technology, Zeromskiego 116, 90-924 Lodz, Poland. zbigniew.draczynski@p.lodz.pl.ORCID 0000-0002-4036-0559
Elzbieta MenaszekDepartment of Cytology, CMUJ-Jagiellonian University Medical College, Swietej Anny 12, 31-008 Krakow, Poland. elzbieta.menaszek@uj.edu.pl.
Ewa Stodolak-ZychAGH-University of Science and Technology, Department of Biomaterials, A. Mickiewicz 30, 30-059 Krakow, Poland. stodolak@agh.edu.pl.ORCID 0000-0002-8935-4811
Marta KaminskaDivision of Biophysics, Institute of Materials Science and Engineering, Lodz University of Technology, Stefanowskiego 1/15, 90-924 Lodz, Poland. marta.kaminska@p.lodz.pl.
Beata KolesinskaInstitute of Organic Chemistry, Lodz University of Technology, Zeromskiego 116, 90-924 Lodz, Poland. beata.kolesinska@p.lodz.pl.ORCID 0000-0002-4581-947X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This study investigates the propensity of short peptides to self-organize and the influence of aggregates on cell cultures. The dipeptides were derived from both enantiomers of identical aromatic amino acids and tripeptides were prepared from two identical aromatic amino acids with one cysteine or methionine residue in the C-terminal, N-terminal, or central position. The formation or absence of fibrous structures under physiological conditions was established using Congo Red and Thioflavine T assays as well as by microscopic examination using normal and polarized light. The in vitro stability of the aggregates in buffered saline solution was assessed over 30 days. Materials with potential for use in regenerative medicine were selected based on the cytotoxicity of the peptides to the endothelial cell line EA.hy 926 and the wettability of the surfaces of the films, as well as using scanning electron microscopy. The criteria were fulfilled by H-

Indexed as

Tissue ScaffoldsAmino AcidsAnimalsBenzothiazolesCell LineCell Line, TumorCell SurvivalCongo RedDipeptidesFibroblastsMiceOligopeptidesProtein AggregatesRegenerative MedicineThiazolesTissue EngineeringAmino AcidsBenzothiazolesCongo RedDipeptidesOligopeptidesProtein AggregatesThiazolesthioflavin Taromatic peptidescytocompatible scaffoldenantiomeric aggregatespeptides self-assemblingregenerative medicine

Identifiers

PMID29498711
PMCPMC6017032

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.