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Surfactant Interactions with Protein-Coated Surfaces: Comparison between Colloidal and Macroscopically Flat Surfaces.
Helena Mateos1, Alessandra Valentini2, Francesco Lopez3
1CSGI (Center for Colloid and Surface Science), via Orabona 4, 70125 Bari, Italy.
Biomimetics (Basel, Switzerland)
|July 8, 2020
Summary
This study compares surfactant interactions with protein-coated silica surfaces of varying curvature. Quantitative agreement was achieved, revealing multilayer formation and different surfactant affinities based on surface geometry.
Area of Science:
- Surface science
- Colloid and interface science
- Biomaterials science
Background:
- Understanding polymer and protein interactions with surfaces is crucial for industrial and biomedical applications.
- Controlling surface modification, cleaning, and biofilm formation relies on managing these interactions.
- The influence of surface geometry on these interactions remains an area of active investigation.
Purpose of the Study:
- To compare surfactant interactions with protein-coated silica surfaces of differing curvature (flat vs. colloidal nanoparticles).
- To investigate the adsorption of bovine serum albumin (BSA) and subsequent surfactant binding on these surfaces.
- To establish quantitative agreement between different measurement techniques across varying geometries.
Main Methods:
- Surface Plasmon Resonance (SPR) to probe interactions with flat silica surfaces.
- Dynamic Light Scattering (DLS) to analyze interactions with colloidal silica nanoparticles (15 nm radius).
- Adsorption studies of BSA followed by non-ionic surfactant (C10PEG8) interaction analysis.
Main Results:
- Quantitative agreement was achieved after correcting SPR data for bound water and DLS data for particle curvature.
- Evidence suggests the formation of surfactant multilayers (C10PEG8) over the protein (BSA) coating.
- Surfactant affinity towards BSA differed significantly depending on whether the protein was on a flat surface or in solution.
Conclusions:
- Surface geometry does not impede quantitative analysis of surfactant-protein interactions when appropriate corrections are applied.
- Multilayer formation of surfactants on protein coatings is supported by the data.
- The affinity of surfactants to proteins is influenced by the protein's surface confinement.
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