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Extending the Range of Controlling Protein Adsorption via Subsurface Architecture
Ezgi Bülbül1,2, Patrick Rupper1, Thomas Geue3
1Laboratory for Advanced Fibers, Empa , Swiss Federal Laboratories for Materials Science and Technology , 9014 St. Gallen , Switzerland.
ACS Applied Materials & Interfaces
|October 24, 2019
Summary
Plasma oxidation modifies subsurface architecture to control protein adsorption. Optimal oxidation time minimizes bovine serum albumin (BSA) adsorption by influencing confined water molecules and their distance.
Area of Science:
- Materials Science
- Surface Chemistry
- Biophysics
Background:
- Confined water in plasma polymer subsurface gradients reduces protein adsorption.
- Hypothesized long-range dipolar field from oriented water interacts with dipolar proteins like bovine serum albumin (BSA).
Purpose of the Study:
- To investigate plasma oxidation modifications of subsurface architecture for enhanced control over protein adsorption.
- To further understand the role of confined water in protein adsorption reduction.
Main Methods:
- In situ multistep plasma deposition and oxidation.
- Neutron reflectivity measurements to analyze matrix-confined water.
Main Results:
- Plasma oxidation increases the amount of matrix-confined water.
- An optimal oxidation time was identified for minimal protein adsorption.
- Minimal distance between confined water molecules appears critical for reducing protein adsorption.
Conclusions:
- Plasma oxidation offers an additional method to control protein adsorption.
- The findings support the hypothesis of water's role in protein adsorption modulation via dipolar interactions.
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