Evidence map›Paper›PMID 40595774›Full record

ArticleScientific reports2025

Characterization of the secondary structure, renaturation and physical ageing of gelatine adhesives.

Elena Pulidori, Celia Duce, Emilia Bramanti, Lidia Ciccone, Brunella Cipolletta, Gloria Tani, Laura Dello Ioio, Leila Birolo, Ilaria Bonaduce

Abstract read
In one paragraph

Article in Scientific reports, 2025. 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. Article
  2. Article
  3. 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

9 authors.

Elena PulidoriDepartment of Chemistry and Industrial Chemistry, University of Pisa, Via G. Moruzzi 13, 56124, Pisa, Italy.
Celia DuceDepartment of Chemistry and Industrial Chemistry, University of Pisa, Via G. Moruzzi 13, 56124, Pisa, Italy. celia.duce@unipi.it.
Emilia BramantiInstitute of Chemistry of Organometallic Compounds, National Research Council, Via G. Moruzzi 1, 56124, Pisa, Italy. emilia.bramanti@pi.iccom.cnr.it.
Lidia CicconeCenter for Instrument Sharing of the University of Pisa (CISUP), University of Pisa, 56126, Pisa, Italy.
Brunella CipollettaDepartment of Chemical Sciences, University of Naples Federico II, Complesso Universitario di Monte S. Angelo, Via Cinthia 21, 80126, Naples, Italy.
Gloria TaniDepartment of Chemistry and Industrial Chemistry, University of Pisa, Via G. Moruzzi 13, 56124, Pisa, Italy.
Laura Dello IoioDello Ioio Restauri, Vico Equense, 80069, Naples, Italy.
Leila BiroloDepartment of Chemical Sciences, University of Naples Federico II, Complesso Universitario di Monte S. Angelo, Via Cinthia 21, 80126, Naples, Italy.
Ilaria BonaduceDepartment of Chemistry and Industrial Chemistry, University of Pisa, Via G. Moruzzi 13, 56124, Pisa, Italy.

Funding

MUR project PRIN 2022 PNRR ArtDECOW P2022HWL7L
6 · The paper itself

Abstract

Animal glues have been used since antiquity, but their popularity decreased in the twentieth century with the rise of synthetic adhesives. Currently they are primarily used in restoration of works of art. This study focuses on animal glue samples derived from bone and hide tissues used mainly for veiling and carpentry applications, examining their secondary structure, thermal and rheological properties, to shed light into their adhesive behaviour. Thermogravimetric analysis and differential scanning calorimetry highlight differences between hide and bone glues, showing that the latter are more hydrolysed. The calorimetric curves show varying values of denaturation enthalpy thus indicating a varying degree of gelatine renaturation. Additionally, the calorimetric analysis demonstrates the physical ageing of the glue samples, which is known to play a key role in maintaining their adhesive properties under specific storage conditions. The rheological data provide fundamental information on properties which are relevant for the use of animal glues as adhesives in various applications. XRD data suggest a low structural order in the samples investigated, where the amorphous component complicates the univocal interpretation of the spectra. FTIR reveal a relatively high content of β-structures in all commercial glue samples, as well as gelatine and collagen standards. Moreover, spectra of the glue films dried for 1 week show that the β-structures are recovered following dissolution in water and application. Therefore, β-structures seem crucial to explain the structure-dependent mechanical properties observed.

Indexed as

AdhesivesGelatinAnimalsCalorimetry, Differential ScanningProtein Structure, SecondaryRheologySpectroscopy, Fourier Transform InfraredThermogravimetryX-Ray DiffractionAdhesivesGelatinAnimal glueGelatineGelatine adhesivesHydrolysed collagenPhysical ageingSecondary structureThermal analysis

Identifiers

PMID40595774
PMCPMC12216275

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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.