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Langmuir : the ACS journal of surfaces and colloids
Apr 05, 2016;32 (13): 3207-16.

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
Author Information
  1. Rami N Foster: National 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.
  2. Elisa T Harrison: National 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.
  3. David G Castner: National 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.
PMID: 26977542 DOI: 10.1021/acs.langmuir.5b04743

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.

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Grants

  1. P41 EB002027/NIBIB NIH HHS
  2. R03 EB014516/NIBIB NIH HHS
  3. EB-002027/NIBIB NIH HHS
  4. EB-014516/NIBIB NIH HHS

MeSH Term

Adsorption
Animals
Cattle
Fibrinogen
Gold
Immunoglobulin G
Photoelectron Spectroscopy
Principal Component Analysis
Serum Albumin, Bovine
Silicon
Spectrometry, Mass, Secondary Ion
Sulfonic Acids
Surface Properties

Chemicals

Immunoglobulin G
Sulfonic Acids
Serum Albumin, Bovine
Gold
Fibrinogen
Silicon
Journal Article Research Support, N.I.H., Extramural

Word Cloud

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