Protein adsorption on nano-patterned hydrogenated amorphous carbon model surfaces

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Predicting how proteins fold and adsorb onto surfaces is a complex problem of strong relevance to the health and environmental sectors. In this work, two nano-patterning techniques, namely focused ion beam (FIB) milling and atomic force microscopy (AFM) nanoindentation were used to develop hydrogenated amorphous carbon (a-C:H) model surfaces with similar nano-topography but different local composition. On the un-patterned surfaces, bovine plasma fibrinogen (BPF) resulted in a thicker and rougher adsorbed film than bovine serum albumin (BSA), although FTIR analysis indicated that, the secondary structure of the proteins changed similarly, with an increase of the -sheet component (+27% and +34% for BSA and BPF, respectively). AFM analysis on the FIB-patterned surfaces indicates that patterning can modify specific protein adsorption behaviors. Moreover, the patterns were compared by imaging the AFM tip/surface adhesive force for BSA adsorbed on either AFM tips or patterned surfaces. The results shows an electrostatic interaction between the implanted Ga+ and BSA surface, modifying the adsorption behavior and the adhesive force. Modelling this interaction gave an estimate of the surface charge per protein, a significantly lower value than in dilute solution (-1.8e instead of -18e). This finding is indicative of protein misfolding, as detected in the FTIR analysis.
LanguageEnglish
Pages239-248
JournalMaterials and Design
Volume97
Issue number5
DOIs
Publication statusPublished - 11 Feb 2016

Fingerprint

Amorphous carbon
Proteins
Adsorption
Bovine Serum Albumin
Atomic force microscopy
Focused ion beams
Fibrinogen
Adhesives
Plasmas
Nanoindentation
Surface charge
Coulomb interactions
Topography
Health
Imaging techniques
Chemical analysis

Keywords

  • Focused ion beam (FIB)
  • Atomic force microscopy (AFM) nanoindentation
  • Nano-patterning
  • Hydrogenated amorphous carbon
  • Protein adsorption

Cite this

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title = "Protein adsorption on nano-patterned hydrogenated amorphous carbon model surfaces",
abstract = "Predicting how proteins fold and adsorb onto surfaces is a complex problem of strong relevance to the health and environmental sectors. In this work, two nano-patterning techniques, namely focused ion beam (FIB) milling and atomic force microscopy (AFM) nanoindentation were used to develop hydrogenated amorphous carbon (a-C:H) model surfaces with similar nano-topography but different local composition. On the un-patterned surfaces, bovine plasma fibrinogen (BPF) resulted in a thicker and rougher adsorbed film than bovine serum albumin (BSA), although FTIR analysis indicated that, the secondary structure of the proteins changed similarly, with an increase of the -sheet component (+27{\%} and +34{\%} for BSA and BPF, respectively). AFM analysis on the FIB-patterned surfaces indicates that patterning can modify specific protein adsorption behaviors. Moreover, the patterns were compared by imaging the AFM tip/surface adhesive force for BSA adsorbed on either AFM tips or patterned surfaces. The results shows an electrostatic interaction between the implanted Ga+ and BSA surface, modifying the adsorption behavior and the adhesive force. Modelling this interaction gave an estimate of the surface charge per protein, a significantly lower value than in dilute solution (-1.8e instead of -18e). This finding is indicative of protein misfolding, as detected in the FTIR analysis.",
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Protein adsorption on nano-patterned hydrogenated amorphous carbon model surfaces. / Mughal, MZ; Lemoine, P; Lubarsky, G; Maguire, PD.

In: Materials and Design, Vol. 97, No. 5, 11.02.2016, p. 239-248.

Research output: Contribution to journalArticle

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AB - Predicting how proteins fold and adsorb onto surfaces is a complex problem of strong relevance to the health and environmental sectors. In this work, two nano-patterning techniques, namely focused ion beam (FIB) milling and atomic force microscopy (AFM) nanoindentation were used to develop hydrogenated amorphous carbon (a-C:H) model surfaces with similar nano-topography but different local composition. On the un-patterned surfaces, bovine plasma fibrinogen (BPF) resulted in a thicker and rougher adsorbed film than bovine serum albumin (BSA), although FTIR analysis indicated that, the secondary structure of the proteins changed similarly, with an increase of the -sheet component (+27% and +34% for BSA and BPF, respectively). AFM analysis on the FIB-patterned surfaces indicates that patterning can modify specific protein adsorption behaviors. Moreover, the patterns were compared by imaging the AFM tip/surface adhesive force for BSA adsorbed on either AFM tips or patterned surfaces. The results shows an electrostatic interaction between the implanted Ga+ and BSA surface, modifying the adsorption behavior and the adhesive force. Modelling this interaction gave an estimate of the surface charge per protein, a significantly lower value than in dilute solution (-1.8e instead of -18e). This finding is indicative of protein misfolding, as detected in the FTIR analysis.

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