Evidence map›Paper›PMID 24282583›Full record

ArticlePloS one2013

Structural determinants for protein adsorption/non-adsorption to silica surface.

Christelle Mathé, Stéphanie Devineau, Jean-Christophe Aude, Gilles Lagniel, Stéphane Chédin, Véronique Legros, Marie-Hélène Mathon, Jean-Philippe Renault, Serge Pin, Yves Boulard and 1 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

28 citing papers in PubMed, 123 citations in OpenAlex.

  1. Article
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  8. Review
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  11. [Advances in separation and analysis of aromatic amino acids in food].Se pu = Chinese journal of chromatography · 2022
    Review
  12. Article
  13. Article
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  15. Article
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  18. Confining a Protein-Containing Water Nanodroplet inside Silica Nanochannels.International journal of molecular sciences · 2019
    Article
  19. Surface Attachment Enhances the Thermodynamic Stability of Protein L.Angewandte Chemie (International ed. in English) · 2019
    Article
  20. 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

11 authors at 5 institutions in 1 country.

Christelle MathéLaboratoire de Radiolyse, SIS2M, IRAMIS and UMR3299 CEA-CNRS, Saclay, France ; Service de Biologie Intégrative et Génétique Moléculaire, iBiTec-S, FRE3377 CEA-CNRS-Université Paris-Sud, Saclay, France ; Laboratoire Analyse et Modélisation pour la Biologie et l'Environnement, UMR 8587 CNRS-Université Evry Val d'Essonne, Evry, France.
Stéphanie Devineau
Jean-Christophe Aude
Gilles Lagniel
Stéphane Chédin
Véronique Legros
Marie-Hélène Mathon
Jean-Philippe Renault
Serge Pin
Yves Boulard
Jean Labarre
CEA Paris-Saclay · FRCentre National de la Recherche Scientifique · FRUniversité Paris-Sud · FRCommissariat à l'Énergie Atomique et aux Énergies Alternatives · FRLaboratoire Analyse et Modélisation pour la Biologie et l'Environnement · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The understanding of the mechanisms involved in the interaction of proteins with inorganic surfaces is of major interest in both fundamental research and applications such as nanotechnology. However, despite intense research, the mechanisms and the structural determinants of protein/surface interactions are still unclear. We developed a strategy consisting in identifying, in a mixture of hundreds of soluble proteins, those proteins that are adsorbed on the surface and those that are not. If the two protein subsets are large enough, their statistical comparative analysis must reveal the physicochemical determinants relevant for adsorption versus non-adsorption. This methodology was tested with silica nanoparticles. We found that the adsorbed proteins contain a higher number of charged amino acids, particularly arginine, which is consistent with involvement of this basic amino acid in electrostatic interactions with silica. The analysis also identified a marked bias toward low aromatic amino acid content (phenylalanine, tryptophan, tyrosine and histidine) in adsorbed proteins. Structural analyses and molecular dynamics simulations of proteins from the two groups indicate that non-adsorbed proteins have twice as many π-π interactions and higher structural rigidity. The data are consistent with the notion that adsorption is correlated with the flexibility of the protein and with its ability to spread on the surface. Our findings led us to propose a refined model of protein adsorption.

Indexed as

AdsorptionElectrophoresis, Gel, Two-DimensionalMicroscopy, Electron, TransmissionProtein ConformationProteinsSilicon DioxideSurface PropertiesProteinsSilicon Dioxide

Identifiers

PMID24282583
PMCPMC3839912
OpenAlexW2089740770

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.