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Tailoring the surface of magnetic microparticles for protein immobilization
Author(s) -
Reichelt Senta,
Elsner Christian,
Pender Alya,
Buchmeiser Michael R.
Publication year - 2011
Publication title -
journal of applied polymer science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.575
H-Index - 166
eISSN - 1097-4628
pISSN - 0021-8995
DOI - 10.1002/app.34153
Subject(s) - chemistry , covalent bond , amine gas treating , protein adsorption , bovine serum albumin , adsorption , polymer chemistry , biomolecule , polyamine , surface modification , desorption , chromatography , organic chemistry , biochemistry
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