Evidence map›Paper›PMID 37890135›Full record

ArticleBiomacromolecules2023

Physicochemical Characterization of a Biomimetic, Elastin-Inspired Polypeptide with Enhanced Thermoresponsive Properties and Improved Cell Adhesion.

Antonella Bandiera, Laura Colomina-Alfaro, Paola Sist, Giovanna Gomez d'Ayala, Federica Zuppardi, Pierfrancesco Cerruti, Ovidio Catanzano, Sabina Passamonti, Ranieri Urbani

Abstract read
In one paragraph

Article in Biomacromolecules, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
  2. Article
  3. 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

9 authors.

Antonella BandieraDepartment of Life Sciences, University of Trieste, via L. Giorgieri, 1, 34127 Trieste, Italy.ORCID 0000-0002-0376-9291
Laura Colomina-AlfaroDepartment of Life Sciences, University of Trieste, via L. Giorgieri, 1, 34127 Trieste, Italy.
Paola SistDepartment of Life Sciences, University of Trieste, via L. Giorgieri, 1, 34127 Trieste, Italy.
Giovanna Gomez d'AyalaInstitute for Polymers, Composites and Biomaterials (IPCB-CNR), Via Campi Flegrei 34, 80078 Pozzuoli, NA, Italy.
Federica ZuppardiInstitute for Polymers, Composites and Biomaterials (IPCB-CNR), Via Campi Flegrei 34, 80078 Pozzuoli, NA, Italy.
Pierfrancesco CerrutiInstitute for Polymers, Composites and Biomaterials (IPCB-CNR), Via Campi Flegrei 34, 80078 Pozzuoli, NA, Italy.
Ovidio CatanzanoInstitute for Polymers, Composites and Biomaterials (IPCB-CNR), Via Campi Flegrei 34, 80078 Pozzuoli, NA, Italy.ORCID 0000-0002-8284-0841
Sabina PassamontiDepartment of Life Sciences, University of Trieste, via L. Giorgieri, 1, 34127 Trieste, Italy.ORCID 0000-0001-7876-4666
Ranieri UrbaniDepartment of Chemical and Pharmaceutical Sciences, University of Trieste, via L. Giorgieri, 1, 34127 Trieste, Italy.ORCID 0000-0002-7802-3697

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Genetic engineering allows fine-tuning and controlling protein properties, thus exploiting the new derivatives to obtain novel materials and systems with improved capacity to actively interact with biological systems. The elastin-like polypeptides are tunable recombinant biopolymers that have proven to be ideal candidates for realizing bioactive interfaces that can interact with biological systems. They are characterized by a thermoresponsive behavior that is strictly related to their peculiar amino acid sequence. We describe here the rational design of a new biopolymer inspired by elastin and the comparison of its physicochemical properties with those of another already characterized member of the same protein class. To assess the cytocompatibility, the behavior of cells of different origins toward these components was evaluated. Our study shows that the biomimetic strategy adopted to design new elastin-based recombinant polypeptides represents a versatile and valuable tool for the development of protein-based materials with improved properties and advanced functionality.

Indexed as

BiomimeticsElastinAmino Acid SequenceBiopolymersCell AdhesionPeptidesBiopolymersElastinPeptides

Identifiers

PMID37890135
PMCPMC10647011

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.