Comparison of Protein-Repellent Behavior of Linear versus Dendrimer-Structured Surface-Immobilized Polymers
| Autor: | Rainer Mueller, Matthias Kronseder, Jutta Lehnfeld, Martina Gruening |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
chemistry.chemical_classification
02 engineering and technology Surfaces and Interfaces Polymer 010402 general chemistry 021001 nanoscience & nanotechnology Condensed Matter Physics 01 natural sciences 0104 chemical sciences chemistry Chemical engineering Dendrimer Electrochemistry General Materials Science 0210 nano-technology Marine industry Spectroscopy Protein adsorption |
| Zdroj: | Langmuir : the ACS journal of surfaces and colloids. 36(21) |
| ISSN: | 1520-5827 |
| Popis: | For many biomedical applications, material surfaces should not only prevent unspecific protein adsorption and bacterial attachment as in many other applications in the food, health, or marine industry, but they should also promote the adhesion of tissue cells. In order to take a first step toward the challenging development of protein and bacteria-repelling and cell-adhesion-promoting materials, polyamine and poly(amido amine) surface coatings with terminal amine groups and varying structure (dendrimer, oligomer, polymer) were immobilized on model surfaces via silane chemistry. Physicochemical analysis showed that all modifications are hydrophilic (contact angles60°) and possess similar surface free energies (SFEs, ∼46-54 mN/m), whereas their amine group densities and zeta potentials at physiological conditions (pH 7.4) varied greatly (-50 to +75 mV). In protein adsorption experiments with single proteins (human serum albumin (HSA) and lysozyme) as well as complex physiological fluids (fetal bovine serum (FBS) and human saliva), the amounts of adsorbed protein were found to correlate strongly with the zeta potential of the surface coatings. Both modifications based on linear polymers exhibited good protein repellency toward all proteins examined and are thus promising for testing in cell adhesion studies. |
| Databáze: | OpenAIRE |
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