Evidence map›Paper›PMID 35498617›Full record

ArticleRSC advances2020

Self-assembled hydrophobic Ala-Aib peptide encapsulating curcumin: a convenient system for water insoluble drugs.

Silvia Locarno, Simona Argentiere, Alessandro Ruffoni, Daniela Maggioni, Raffaella Soave, Raffaella Bucci, Emanuela Erba, Cristina Lenardi, Maria Luisa Gelmi, Francesca Clerici

Abstract read
In one paragraph

Article in RSC advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. Article
  3. Amphiphilic Polyethylene-International journal of molecular sciences · 2023
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. 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

10 authors.

Silvia LocarnoDepartment of Pharmaceutical Sciences, General and Organic Chemistry Section "A. Marchesini", University of Milan Via Venezian 21 20133 Milano Italy francesca.clerici@unimi.it.ORCID https://orcid.org/0000-0003-1385-7137
Simona ArgentiereCIMAINA, Interdisciplinary Center for Nanostructured Materials and Interfaces, Department of Physics Via Celoria 16 20133 Milano Italy.
Alessandro RuffoniSchool of Chemistry, University of Manchester Manchester M13 9PL UK.ORCID https://orcid.org/0000-0001-8617-2548
Daniela MaggioniDepartment of Chemistry, Università Degli Studi di Milano Via Golgi 19 20133 Milano Italy.ORCID https://orcid.org/0000-0001-5201-4824
Raffaella SoaveInstitute of Chemical Sciences and Technologies "Giulio Natta", Italian National Research Council, CNR-SCITEC Via Golgi 19 20133 Milano Italy.ORCID https://orcid.org/0000-0003-4909-651X
Raffaella BucciDepartment of Pharmaceutical Sciences, General and Organic Chemistry Section "A. Marchesini", University of Milan Via Venezian 21 20133 Milano Italy francesca.clerici@unimi.it.
Emanuela ErbaDepartment of Pharmaceutical Sciences, General and Organic Chemistry Section "A. Marchesini", University of Milan Via Venezian 21 20133 Milano Italy francesca.clerici@unimi.it.
Cristina LenardiCIMAINA, Interdisciplinary Center for Nanostructured Materials and Interfaces, Department of Physics Via Celoria 16 20133 Milano Italy.
Maria Luisa GelmiDepartment of Pharmaceutical Sciences, General and Organic Chemistry Section "A. Marchesini", University of Milan Via Venezian 21 20133 Milano Italy francesca.clerici@unimi.it.ORCID https://orcid.org/0000-0003-0743-5499
Francesca ClericiDepartment of Pharmaceutical Sciences, General and Organic Chemistry Section "A. Marchesini", University of Milan Via Venezian 21 20133 Milano Italy francesca.clerici@unimi.it.ORCID https://orcid.org/0000-0003-3483-5914

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The exploitation of self-assembled systems to improve the solubility of drugs is getting more and more attention. Among the different types of self-assembled biomaterials, peptides and in particular peptides containing non-coded amino acids (NCAPs) are promising because their use opens the door to more stable materials inducing increased stability to proteolysis. New classes of NCAP, Ac-Ala-X-Ala-Aib-AlaCONH

Identifiers

PMID35498617
PMCPMC9050355

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.