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Abstract
Polysiloxane microspheres containing a large number of silanol groups were functionalized by reactions of these groups with organic alkoxy or chlorosilanes having chloro, amine or imidazole functions in their organic parts. The obtained imidazole groups on the microspheres were ionized by the reaction with n-octyl iodide and with methyl iodide while the chloro functions were used for quaternization of a tertiary amine. Adsorption of gamma globulins on these functionalized microspheres was studied in aqueous suspension at pH 5.2, 7.4 and 9.2. Hydrophilic–hydrophobic properties of these microspheres were examined by measuring adsorption of a hydrophobic dye, Rose Bengal. The functionalized microspheres showed higher adsorption of globulins and higher hydrophobicity than the not functionalized ones rich in silanol groups. In the case of microspheres with ionic functional groups the electrostatic forces also contribute to attractive interactions between proteins and microspheres.
Highlights
Proteins show a large affinity to surfaces of various silicone materials
It is generally accepted that the adsorption of proteins on non-polar surfaces is mostly controlled by hydrophobic-hydrophilic properties of the surface [4, 5]
J Inorg Organomet Polym (2015) 25:507–514 number of silicon atoms in these particles. We found that these particles are highly hydrophilic and do not adsorb a hydrophobic dye Rose Bengal from its aqueous solution [21]
Summary
Adsorption of proteins on these surfaces occurs instantly whenever silicones are exposed to biological medium [1, 2]. This phenomenon is a very common one and has a great impact on biomedical and biotechnical applications of silicone materials [2,3,4]. It is generally accepted that the adsorption of proteins on non-polar surfaces is mostly controlled by hydrophobic-hydrophilic properties of the surface [4, 5] These properties may be tuned by functionalization of surfaces. It was noticed that presence of ionic groups on surface of polysiloxane may lead to important contribution of electrostatic interaction to the driving force of protein adsorption [16, 19]
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