Evidence map›Paper›PMID 34203919›Full record

ArticleBiomedicines2021

Self-Supporting Hydrogels Based on Fmoc-Derivatized Cationic Hexapeptides for Potential Biomedical Applications.

Carlo Diaferia, Elisabetta Rosa, Enrico Gallo, Giovanni Smaldone, Mariano Stornaiuolo, Giancarlo Morelli, Antonella Accardo

Abstract read
In one paragraph

Article in Biomedicines, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Article
  2. Self-Assembly of Peptides and Biomolecular Systems Into Functional Nanomaterials.Journal of peptide science : an official publication of the European Peptide Society · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
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  11. Article
  12. 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

7 authors.

Carlo DiaferiaDepartment of Pharmacy and Research Centre on Bioactive Peptides (CIRPeB), University of Naples "Federico II", 80134 Naples, Italy.ORCID 0000-0002-9273-0136
Elisabetta RosaDepartment of Pharmacy and Research Centre on Bioactive Peptides (CIRPeB), University of Naples "Federico II", 80134 Naples, Italy.
Enrico GalloIRCCS SDN, Via Gianturco 113, 80143 Naples, Italy.
Giovanni SmaldoneIRCCS SDN, Via Gianturco 113, 80143 Naples, Italy.ORCID 0000-0002-1989-4740
Mariano StornaiuoloDepartment of Pharmacy and Research Centre on Bioactive Peptides (CIRPeB), University of Naples "Federico II", 80134 Naples, Italy.ORCID 0000-0003-2200-5083
Giancarlo MorelliDepartment of Pharmacy and Research Centre on Bioactive Peptides (CIRPeB), University of Naples "Federico II", 80134 Naples, Italy.
Antonella AccardoDepartment of Pharmacy and Research Centre on Bioactive Peptides (CIRPeB), University of Naples "Federico II", 80134 Naples, Italy.ORCID 0000-0002-7899-2359

Funding

Ministero dell'Istruzione, dell'Università e della Ricerca B61G18000470007
6 · The paper itself

Abstract

Peptide-based hydrogels (PHGs) are biocompatible materials suitable for biological, biomedical, and biotechnological applications, such as drug delivery and diagnostic tools for imaging. Recently, a novel class of synthetic hydrogel-forming amphiphilic cationic peptides (referred to as series K), containing an aliphatic region and a Lys residue, was proposed as a scaffold for bioprinting applications. Here, we report the synthesis of six analogues of the series K, in which the acetyl group at the N-terminus is replaced by aromatic portions, such as the Fmoc protecting group or the Fmoc-FF hydrogelator. The tendency of all peptides to self-assemble and to gel in aqueous solution was investigated using a set of biophysical techniques. The structural characterization pointed out that only the Fmoc-derivatives of series K keep their capability to gel. Among them, Fmoc-K3 hydrogel, which is the more rigid one (G' = 2526 Pa), acts as potential material for tissue engineering, fully supporting cell adhesion, survival, and duplication. These results describe a gelification process, allowed only by the correct balancing among aggregation forces within the peptide sequences (e.g., van der Waals, hydrogen bonding, and π-π stacking).

Indexed as

Fmoc peptidespeptide hydrogelpeptide materialsself-assemblingtissue engineering

Identifiers

PMID34203919
PMCPMC8232644

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.