Evidence map›Paper›PMID 24780165›Full record

ArticleBiomaterials2014

Effect of the interplay between protein and surface on the properties of adsorbed protein layers.

Myriam M Ouberai, Kairuo Xu, Mark E Welland

Abstract read
In one paragraph

Article in Biomaterials, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Prospects and challenges of recombinant spider venom enzymes: insights fromFrontiers in bioengineering and biotechnology · 2025
    Article
  5. Review
  6. Article
  7. Quartz Crystal Microbalance Application andLangmuir : the ACS journal of surfaces and colloids · 2023
    Article
  8. Article
  9. Next-generation biomaterials for dental pulp tissue immunomodulation.Dental materials : official publication of the Academy of Dental Materials · 2023
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Dielectric Spectroscopy Can Predict the Effect of External AC Fields on the Dynamic Adsorption of Lysozyme.Chemphyschem : a European journal of chemical physics and physical chemistry · 2022
    Article
  15. Selective Separation of Highly Similar Proteins on Ionic Liquid-Loaded Mesoporous TiOLangmuir : the ACS journal of surfaces and colloids · 2022
    Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Biomaterial-directed cell behavior for tissue engineering.Current opinion in biomedical engineering · 2021
    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

3 authors.

Myriam M OuberaiNanoscience Centre, Department of Engineering, University of Cambridge, Cambridge CB3 0FF, UK. Electronic address: mmo25@cam.ac.uk.
Kairuo XuNanoscience Centre, Department of Engineering, University of Cambridge, Cambridge CB3 0FF, UK.
Mark E WellandNanoscience Centre, Department of Engineering, University of Cambridge, Cambridge CB3 0FF, UK.

Funding

Biotechnology and Biological Sciences Research Council BB/H003843/1
6 · The paper itself

Abstract

Although protein adsorption to surface is a common phenomenon, investigation of the process is challenging due to the complexity of the interplay between external factors, protein and surface properties. Therefore experimental approaches have to measure the properties of adsorbed protein layers with high accuracy in order to achieve a comprehensive description of the process. To this end, we used a combination of two biosensing techniques, dual polarization interferometry and quartz crystal microbalance with dissipation. From this, we are able to extract surface coverage values, layer structural parameters, water content and viscoelastic properties to examine the properties of protein layers formed at the liquid/solid interface. Layer parameters were examined upon adsorption of proteins of varying size and structural properties, on surfaces with opposite polarity. We show that "soft" proteins such as unfolded α-synuclein and high molecular weight albumin are highly influenced by the surface polarity, as they form a highly diffuse and hydrated layer on the hydrophilic silica surface as opposed to the denser, less hydrated layer formed on a hydrophobic methylated surface. These layer properties are a result of different orientations and packing of the proteins. By contrast, lysozyme is barely influenced by the surface polarity due to its intrinsic structural stability. Interestingly, we show that for a similar molecular weight, the unfolded α-synuclein forms a layer with the highest percentage of solvation not related to surface coverage but resulting from the highest water content trapped within the protein. Together, these data reveal a trend in layer properties highlighting the importance of the interplay between protein and surface for the design of biomaterials.

Indexed as

AdsorptionAnimalsBuffersCattleHumansInterferometryMuramidaseQuartz Crystal Microbalance TechniquesSerum Albumin, BovineShear StrengthSurface PropertiesBuffersMuramidaseSerum Albumin, BovineDPILayer propertiesPercentage solvationProtein adsorptionQCM-DViscoelastic property

Identifiers

PMID24780165
PMCPMC4051990

What OpenQuestion holds

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LicenceCC BY
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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.