Abstract
In-situ attenuated total reflection (ATR)-FTIR spectroscopy enabled studies on the interaction between the differently charged model proteins human serum albumin, lysozyme, immunoglobulin G and multilayer assemblies, which were deposited by alternating adsorption of poly(ethyleneimine) and poly(acrylic acid) onto Si crystals. Low adsorbed protein amounts were observed if the top polyelectrolyte layer and the protein were equally charged, whereas enhanced protein adsorption occurred for electrostatic attraction between protein and top polyelectrolyte layer.
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