Evidence map›Paper›PMID 26977542›Full record

ArticleLangmuir : the ACS journal of surfaces and colloids2016

ToF-SIMS and XPS Characterization of Protein Films Adsorbed onto Bare and Sodium Styrenesulfonate-Grafted Gold Substrates.

Rami N Foster, Elisa T Harrison, David G Castner

Abstract read
In one paragraph

Article in Langmuir : the ACS journal of surfaces and colloids, 2016. 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
–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

17 citing papers in PubMed.

  1. Article
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  3. Article
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  8. Developments and Ongoing Challenges for Analysis of Surface-Bound Proteins.Annual review of analytical chemistry (Palo Alto, Calif.) · 2021
    Article
  9. Article
  10. Review
  11. Surface Analysis: From Single Crystals to Biomaterials.Surface and interface analysis : SIA · 2018
    Article
  12. Article
  13. Review
  14. Article
  15. Article
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  17. Review
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.

Rami N FosterNational ESCA and Surface Analysis Center for Biomedical Problems, Department of Chemical Engineering, and ‡National ESCA and Surface Analysis Center for Biomedical Problems, Department of Bioengineering, University of Washington , Seattle, Washington 98195, United States.
Elisa T HarrisonNational ESCA and Surface Analysis Center for Biomedical Problems, Department of Chemical Engineering, and ‡National ESCA and Surface Analysis Center for Biomedical Problems, Department of Bioengineering, University of Washington , Seattle, Washington 98195, United States.
David G CastnerNational ESCA and Surface Analysis Center for Biomedical Problems, Department of Chemical Engineering, and ‡National ESCA and Surface Analysis Center for Biomedical Problems, Department of Bioengineering, University of Washington , Seattle, Washington 98195, United States.

Funding

Surface Analysis Facility for Biomedical ProblemsP41EB002027 · NIBIB · UNIVERSITY OF WASHINGTON · PI CASTNER, DAVID G · 2003 to 2019
$17.6M
Computational tools for the prediction of protein orientations on material surfacR03EB014516 · NIBIB · UNIVERSITY OF WASHINGTON · PI THOMAS, WENDY E · 2013 to 2014
$152k
NIBIB NIH HHS EB-002027NIBIB NIH HHS EB-014516NIBIB NIH HHS P41 EB002027NIBIB NIH HHS R03 EB014516
6 · The paper itself

Abstract

The adsorption of single-component bovine serum albumin (BSA), bovine fibrinogen (Fgn), and bovine immunoglobulin G (IgG) films as well as multicomponent bovine plasma films onto bare and sodium styrenesulfonate (NaSS)-grafted gold substrates was characterized. The adsorption isotherms, measured via X-ray photoelectron spectroscopy, showed that at low solution concentrations all three single-component proteins adsorb with higher affinity onto gold surfaces compared to NaSS surfaces. However, at higher concentrations, NaSS surfaces adsorb the same or more total protein than gold surfaces. This may be because proteins that adsorb onto NaSS undergo structural rearrangements, resulting in a larger fraction of irreversibly adsorbed species over time. Still, with the possible exception of BSA adsorbed onto gold, neither surface appeared to have saturated at the highest protein solution concentration studied. Principal component (PC) analysis of amino acid mass fragments from time-of-flight secondary ion mass spectra distinguished between the same protein adsorbed onto NaSS and gold surfaces, suggesting that proteins adsorb differently on NaSS and gold surfaces. Explored further using peak ratios for buried/surface amino acids for each protein, we found that proteins denature more on NaSS surfaces than on gold surfaces. Also, using peak ratios for asymmetrically distributed amino acids, potential structural differences were postulated for BSA and IgG adsorbed onto NaSS and gold surfaces. PC modeling, used to track changes in plasma adsorption with time, suggests that plasma films on NaSS and Au surfaces become more Fgn-like with increasing adsorption time. However, the PC models included only three proteins, where plasma is composed of hundreds of proteins. Therefore, while both gold and NaSS appear to adsorb more Fgn with time, further study is required to confirm that this is representative of the final state of the plasma films.

Indexed as

AdsorptionAnimalsCattleFibrinogenGoldImmunoglobulin GPhotoelectron SpectroscopyPrincipal Component AnalysisSerum Albumin, BovineSiliconSpectrometry, Mass, Secondary IonSulfonic AcidsSurface PropertiesFibrinogenGoldImmunoglobulin GSerum Albumin, BovineSiliconSulfonic Acids

Identifiers

PMID26977542
PMCPMC4821661

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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.