Evidence map›Paper›PMID 32275138›Full record

ArticleBiomacromolecules2020

Role of Sheet-Edge Interactions in β-sheet Self-Assembling Peptide Hydrogels.

Jacek K Wychowaniec, Andrew M Smith, Cosimo Ligorio, Oleksandr O Mykhaylyk, Aline F Miller, Alberto Saiani

Abstract read
In one paragraph

Article in Biomacromolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed.

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  7. RGD-functionalised self-assembling peptide hydrogel induces a proliferative profile in human osteoblasts in vitro.Journal of peptide science : an official publication of the European Peptide Society · 2025
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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

6 authors.

Jacek K WychowaniecSchool of Materials, The University of Manchester, Oxford Road, M13 9PL Manchester, U.K.ORCID 0000-0002-6597-5242
Andrew M SmithSchool of Materials, The University of Manchester, Oxford Road, M13 9PL Manchester, U.K.
Cosimo LigorioSchool of Materials, The University of Manchester, Oxford Road, M13 9PL Manchester, U.K.ORCID 0000-0001-5917-4652
Oleksandr O MykhaylykSoft Matter Analytical Laboratory, Dainton Building, Department of Chemistry, The University of Sheffield, Sheffield S3 7HF, U.K.ORCID 0000-0003-4110-8328
Aline F MillerManchester Institute of Biotechnology, The University of Manchester, Oxford Road, M13 9PL Manchester, U.K.
Alberto SaianiSchool of Materials, The University of Manchester, Oxford Road, M13 9PL Manchester, U.K.ORCID 0000-0002-5504-8306

Funding

Medical Research Council
6 · The paper itself

Abstract

Hydrogels' hydrated fibrillar nature makes them the material of choice for the design and engineering of 3D scaffolds for cell culture, tissue engineering, and drug-delivery applications. One particular class of hydrogels which has been the focus of significant research is self-assembling peptide hydrogels. In the present work, we were interested in exploring how fiber-fiber edge interactions affect the self-assembly and gelation properties of amphipathic peptides. For this purpose, we investigated two β-sheet-forming peptides, FEFKFEFK (F8) and KFEFKFEFKK (KF8K), the latter one having the fiber edges covered by lysine residues. Our results showed that the addition of the two lysine residues did not affect the ability of the peptides to form β-sheet-rich fibers, provided that the overall charge carried by the two peptides was kept constant. However, it did significantly reduce edge-driven hydrophobic fiber-fiber associative interactions, resulting in reduced tendency for KF8K fibers to associate/aggregate laterally and form large fiber bundles and consequently network cross-links. This effect resulted in the formation of hydrogels with lower moduli but faster dynamics. As a result, KF8K fibers could be aligned only under high shear and at high concentration while F8 hydrogel fibers were found to align readily at low shear and low concentration. In addition, F8 hydrogels were found to fragment at high concentration because of the high aggregation state stabilizing the fiber bundles, resulting in fiber breakage rather than disentanglement and alignment.

Indexed as

HydrogelsPeptidesHydrophobic and Hydrophilic InteractionsProtein Conformation, beta-StrandTissue EngineeringHydrogelsPeptides

Identifiers

PMID32275138
PMCPMC7304824

What OpenQuestion holds

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Registered trials

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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.