| Popis: |
Magnetic, amine-functionalized microparticles (dynabeads®) were surface-modified with different polyamines to suppress the nonspecific protein adsorption to a maximum extent but to allow for the enhanced covalent attachment of selected biomolecules (proteins). The stepwise chemical modification entailed the consecutive reaction of amine-functionalized dynabeads® with glutaric dialdehyde (GA) followed by the reaction with multifunctional, amine-containing compounds such as poly(allyl amine), poly(ethylene imine), and bovine serum albumin. The model proteins trypsin and concanavalin A, respectively, were finally covalently bound to the polyamine-functionalized dynabeads via GA-mediated coupling. Matrix-assisted laser-desorption/ionization time of flight/time of flight mass spectrometry confirmed the successful protein attachment. Both the nonspecific protein adsorption to the different polyamine-modified surfaces and the GA-mediated covalent binding of the target proteins to the polyamine-functionalized surfaces was quantified by standard bioassays. Compared to unmodified beads, the bioactivity of the polyamine-functionalized ones was increased by a factor of seven while keeping the nonspecific protein adsorption of a selected cationic protein at a very low level. © 2011 Wiley Periodicals, Inc. J Appl Polym Sci, 2011 |
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