Adsorption of the Flexible Salivary Proteins Statherin and PRP-1 to Negatively Charged Surfaces – A Monte Carlo Simulation and Ellipsometric Study
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Marie Skepö
The structural properties of the salivary proteins, acidic proline rich PRP-1 and statherin, adsorbed onto negatively charged surfaces have been studied by Monte Carlo simulations and ellipsometry. It is shown that both proteins adsorb to negatively charged surfaces, although their net charges are negative. Experimentally, an initial fast mass-controlled film build-up was detected for both proteins, and plateaus were reached within 10 min. The isotherm shape and the adsorbed amounts were similar for PRP-1 to hydrophilic and hydrophobic surfaces, while statherin adsorbs to a greater extent to the hydrophobic surface. These results could be explained from the simulation results by considering the proteins as diblock polyampholytes. It has also been shown that the adsorption of PRP-1 to a negatively charged surface may be purely electrostatically driven, while pure electrostatic interaction is not sufficient to drive adsorption of statherin, i.e., an extra short-ranged attractive interaction is necessary to account for the experimental observations.
© Oldenbourg Wissenschaftsverlag
Articles in the same Issue
- Bunsen Colloquium: Controlling Protein Adsorption at Materials Surfaces
- Adsorption of Collagen Fragments on Titanium Oxide Surfaces: A Molecular Dynamics Study
- Adsorption of the Flexible Salivary Proteins Statherin and PRP-1 to Negatively Charged Surfaces – A Monte Carlo Simulation and Ellipsometric Study
- Surface-Tethered Polymers to Influence Protein Adsorption and Microbial Adhesion
- Lactoperoxidase and Histatin 5 – their Adsorption Behaviour on Silica and Hydrophobized Silica Surfaces, and Implications on their Role in the Initial Salivary Film Formation
- Ultrasensitive Fluorescence Microscopy Studies of Protein Interactions with Functionalized Surfaces
- Adsorption of Amyloid β (1-40) Peptide at Liquid Interfaces
- Controlled Release of Proteins Bound to Spherical Polyelectrolyte Brushes
- In-Situ-ATR-FTIR Detection of Protein Sorption at Polyelectrolyte Multilayers: Variation of the Thickness
- Stability of Proteins Confined in MCM-48 Mesoporous Molecular Sieves – The Effects of pH, Temperature and Co-solvents
- Hydrogen Bonding of Water Confined in Controlled-Pore Glass 10-75 Studied by 1H-Solid State NMR
Articles in the same Issue
- Bunsen Colloquium: Controlling Protein Adsorption at Materials Surfaces
- Adsorption of Collagen Fragments on Titanium Oxide Surfaces: A Molecular Dynamics Study
- Adsorption of the Flexible Salivary Proteins Statherin and PRP-1 to Negatively Charged Surfaces – A Monte Carlo Simulation and Ellipsometric Study
- Surface-Tethered Polymers to Influence Protein Adsorption and Microbial Adhesion
- Lactoperoxidase and Histatin 5 – their Adsorption Behaviour on Silica and Hydrophobized Silica Surfaces, and Implications on their Role in the Initial Salivary Film Formation
- Ultrasensitive Fluorescence Microscopy Studies of Protein Interactions with Functionalized Surfaces
- Adsorption of Amyloid β (1-40) Peptide at Liquid Interfaces
- Controlled Release of Proteins Bound to Spherical Polyelectrolyte Brushes
- In-Situ-ATR-FTIR Detection of Protein Sorption at Polyelectrolyte Multilayers: Variation of the Thickness
- Stability of Proteins Confined in MCM-48 Mesoporous Molecular Sieves – The Effects of pH, Temperature and Co-solvents
- Hydrogen Bonding of Water Confined in Controlled-Pore Glass 10-75 Studied by 1H-Solid State NMR
