Evidence map›Paper›PMID 37238645›Full record

ArticleBiomolecules2023

Physico-Chemical Changes Induced by Gamma Irradiation on Some Structural Protein Extracts.

Maria Stanca, Carmen Gaidau, Traian Zaharescu, George-Alin Balan, Iulia Matei, Aurica Precupas, Anca Ruxandra Leonties, Gabriela Ionita

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.0field-weighted citation impact, top 15% of its field
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

14 citing papers in PubMed, 20 citations in OpenAlex.

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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

8 authors at 2 institutions in 1 country.

Maria StancaLeather Research Department, Research and Development National Institute for Textiles and Leather-Division Leather and Footwear Research Institute, 93, Ion Minulescu Street, 031215 Bucharest, Romania.ORCID 0000-0002-8920-9040
Carmen GaidauLeather Research Department, Research and Development National Institute for Textiles and Leather-Division Leather and Footwear Research Institute, 93, Ion Minulescu Street, 031215 Bucharest, Romania.ORCID 0000-0003-1961-0178
Traian ZaharescuINCDIE ICPE CA, 313 Splaiul Unirii, 030138 Bucharest, Romania.ORCID 0000-0002-1030-7511
George-Alin Balan"Ilie Murgulescu" Institute of Physical Chemistry of the Romanian Academy, 202 Splaiul Independentei, 060021 Bucharest, Romania.ORCID 0000-0003-4653-7025
Iulia Matei"Ilie Murgulescu" Institute of Physical Chemistry of the Romanian Academy, 202 Splaiul Independentei, 060021 Bucharest, Romania.ORCID 0000-0003-4611-9405
Aurica Precupas"Ilie Murgulescu" Institute of Physical Chemistry of the Romanian Academy, 202 Splaiul Independentei, 060021 Bucharest, Romania.ORCID 0000-0002-2381-7617
Anca Ruxandra Leonties"Ilie Murgulescu" Institute of Physical Chemistry of the Romanian Academy, 202 Splaiul Independentei, 060021 Bucharest, Romania.ORCID 0000-0001-5989-4633
Gabriela IonitaLeather Research Department, Research and Development National Institute for Textiles and Leather-Division Leather and Footwear Research Institute, 93, Ion Minulescu Street, 031215 Bucharest, Romania.ORCID 0000-0001-9235-9093
Romanian Academy · RONational Research & Development Institute for Textiles and Leather · RO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this study, the effect of gamma irradiation (10 kGy) on proteins extracted from animal hide, scales, and wool was evidenced by calorimetric (μDSC) and spectroscopic (IR, circular dichroism, and EPR) methods. Keratin was obtained from sheep wool, collagen and bovine gelatin from bovine hide, and fish gelatin from fish scales. The μDSC experiments evidenced that gamma irradiation influences the thermal stability of these proteins differently. The thermal stability of keratin decreases, while a resistance to thermal denaturation was noticed for collagen and gelatins after gamma irradiation. The analysis of the IR spectra demonstrated that gamma irradiation determines changes in the vibrational modes of the amide groups that are associated with protein denaturation, most meaningfully in the case of keratin. As evidenced by circular dichroism for all proteins considered, exposure to gamma radiation produces changes in the secondary structure that are more significant than those produced by UV irradiation. Riboflavin has different effects on the secondary structure of the investigated proteins, a stabilizing effect for keratin and fish gelatin and a destabilizing effect for bovine gelatin, observed in both irradiated and non-irradiated samples. The EPR spectroscopy evidences the presence, in the gamma-irradiated samples, of free radicals centered on oxygen, and the increase in their EPR signals over time due to the presence of riboflavin.

Indexed as

CollagenGelatinAnimalsCattleCircular DichroismElectron Spin Resonance SpectroscopyKeratinsSheepCollagenGelatinKeratinsbovine gelatincircular dichroism spectroscopycollagenEPR spectroscopyfish gelatinIR spectroscopykeratinriboflavinμDSC

Identifiers

PMID37238645
PMCPMC10216533
OpenAlexW4367625307

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.