Adsorption of Collagen Fragments on Titanium Oxide Surfaces: A Molecular Dynamics Study
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Susan Köppen
The adsorption of flexible collagen I triple helices with lengths of 8 nm in aqueous solution on a partially hydroxylated rutile layer (pH = 7.4) is modelled by classical molecular dynamics simulation with trajectories of up to 5 ns lengths. The carboxyl groups of glutamic and aspartic acids form hydrogen bonds with surface protons, which result in stable contact points at 300 K, if the bond length is smaller than 2 Å. Lysine side chains bind to surface hydroxyl groups. In spite of rotational motion around the C–N figure axis and opening and closing of hydrogen bonds, the amino groups are immobilized at the surface at N–O distances below 4 Å. In all runs the proteins have few contact points to the surface even though it is perfectly planar in our simulation. We suggest that the experimentally observed increase of adsorption energy and area per molecule over time may be associated to an increase of the number of contact points, which induces spreading of the adsorbate.
© 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
