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Modulation of Proteins Adsorption onto the Surface of Chitosan Complexed with Anionic Copolymers. Real Time Analysis by Surface Plasmon Resonance
Author(s) -
Aguilar María R.,
Gallardo Alberto,
Lechuga Laura M.,
Calle Ana,
San Román Julio
Publication year - 2004
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/mabi.200400039
Subject(s) - chemistry , surface plasmon resonance , adsorption , chitosan , polyacrylic acid , polyelectrolyte , aqueous solution , polymer chemistry , acrylic acid , protein adsorption , copolymer , sulfonic acid , chemical engineering , polymer , organic chemistry , nanoparticle , engineering
Summary: The interpolyelectrolyte complex formation between chitosan and anionic polyacrylic derivatives, bearing sulfonic moieties, as well as the protein adsorption onto the chitosan/polyacrylic complexes were studied by surface plasmon resonance (SPR) optical biosensor. This unique technique allows a real time monitoring of different surface molecular interactions with very high sensitivity. The acrylic macromolecules are two families of copolymers of 2‐acrylamido‐2‐methylpropane sulfonic acid (AMPS) and, respectively, 2‐hydroxyethylmethacrylate (HEMA) and N , N′ ‐dimethylacrylamide (DMAA). The complexation process was evaluated through the SPR measurements resulting from the flowing of polyacrylic aqueous solution over the sensor previously coated with chitosan. The SPR was able to differentiate strong ionic bonds from other weak and reversible interactions. By means of the coated sensors (uncomplexed and the whole series of complexed chitosan), SPR cold be used for a simple “in vitro” protein adsorption analysis, by flowing aqueous solutions of albumin and fibrinogen. While both proteins were adsorbed on the uncomplexed chitosan, the complexed coatings exhibited different and very promising behaviors. In particular, they showed no adsorption or only selective adsorption of albumin.A SPR experimental set‐up in the Kretschmann configuration.