Controlled Release of Proteins Bound to Spherical Polyelectrolyte Brushes
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A. Wittemann
We discuss the interaction of proteins dissolved in aqueous solution with spherical polyelectrolyte brushes (SPB). The SPB consist of a solid core particle of colloidal dimensions (ca. 100 nm in diameter) onto which long polyelectrolyte chains have been grafted. Immersed in aqueous solution of proteins these SPB will take up high amounts of protein if the ionic strength is low. At high ionic strength, however, virtually no protein will enter into the brush layer attached to the surface of the core particles. We show that bovine serum albumin (BSA) bound at low ionic strength will gradually be released upon raising the salt concentration in the solution in a well-controlled manner: For each raise of the ionic strength in solution there is a well-defined amount of protein that is released. We show that BSA adsorbed to a conventional carboxylated latex will not be released if treated in the same manner. All findings, namely the uptake of protein as well as the controlled release can be explained by the “counterion release force”: Patches of positive charge on the surface of the proteins which are immersed in the brush layer become multivalent counterions of the polyelectrolyte chains thus releasing a concomitant number of counter- and coions. Release of counterions as induced by the adsorption of proteins is hence the main driving force for the polyelectrolyte-mediated protein adsorption (PMPA).
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Artikel in diesem Heft
- 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
