Evidence map›Paper›PMID 32778712›Full record

ArticleScientific reports2020

The molecular insights into protein adsorption on hematite surface disclosed by in-situ ATR-FTIR/2D-COS study.

Matheus Sampaio C Barreto, Evert J Elzinga, Luís Reynaldo F Alleoni

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.2field-weighted citation impact, top 9% 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

17 citing papers in PubMed, 74 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

3 authors at 3 institutions in 3 countries.

Matheus Sampaio C BarretoAgroBiosciences Division, Mohammed VI Polytechnic University (UM6P), Lot 660, Hay Moulay Rachid, 43150, Benguerir, Morocco. matheus.barreto.ufv@gmail.com.
Evert J ElzingaDepartment of Earth & Environmental Sciences, Rutgers University, Newark, NJ, USA.
Luís Reynaldo F AlleoniDepartment of Soil Science, Luiz de Queiroz College of Agriculture (ESALQ), University of São Paulo (USP), Piracicaba, SP, Brazil.
Rutgers, The State University of New Jersey · USUniversidade de São Paulo · BRUniversité Mohammed VI Polytechnique · MA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins are of ubiquitous interest in the Life Sciences but are of interest in the Geosciences as well because of the significant role these compounds play in the biogeochemical cycling of trace and nutrient elements. Structural changes resulting from the adsorption of proteins onto mineral surfaces may alter protein biological function and other environmental interactions. Iron oxides are major sinks of a range of environmental elements including organic compounds. In this study, the adsorption of the broadly studied model protein BSA onto the hematite mineral surface was characterized as a function of pH, ionic strength, and BSA concentration using in-situ Attenuated Total Reflection Fourier Transform Infrared (ATR-FTIR) spectroscopy. BSA lost the α-helix and gain β-sheets in the secondary structure during adsorption on hematite. BSA adsorption was maximum at pH 5, a value close to the BSA isoelectric point (~ pH 5), and lower at pH 4 and pH 7. Increasing ionic strength decreased to total BSA adsorption. Two-dimensional correlation spectroscopy analysis of the ATR-FTIR spectra revealed that higher initial BSA concentration and the consequent higher BSA surface loading enhanced BSA adsorption by protein-protein interaction, which less ordered structures changes into more compact forms decrease, hence compacting the structural arrangement and could promoting multilayers/aggregation formation on the mineral surface. The activity of enzymes following adsorption on mineral surfaces requires further study.

Indexed as

AdsorptionFerric CompoundsFourier AnalysisHydrogen-Ion ConcentrationIsoelectric PointProtein ConformationProteinsProtein Structure, SecondarySerum Albumin, BovineSpectroscopy, Fourier Transform InfraredSurface PropertiesFerric Compoundsferric oxideProteinsSerum Albumin, Bovine

Identifiers

PMID32778712
PMCPMC7417568
OpenAlexW3048139788

What OpenQuestion holds

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LicenceCC BY
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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.