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In Situ ATR‐FTIR Spectroscopy on the Deposition and Protein Interaction of Polycation/Alginate Multilayers
Author(s) -
Müller Martin,
Torger Bernhard,
Keßler Bernd
Publication year - 2010
Publication title -
advanced engineering materials
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.938
H-Index - 114
eISSN - 1527-2648
pISSN - 1438-1656
DOI - 10.1002/adem.201080059
Subject(s) - polyelectrolyte , chemical engineering , fourier transform infrared spectroscopy , chitosan , materials science , protein adsorption , adsorption , human serum albumin , ethyleneimine , spectroscopy , polymer chemistry , chemistry , polymer , organic chemistry , chromatography , physics , quantum mechanics , engineering , composite material
We report in situ ATR‐FTIR spectroscopy studies of the deposition of biocompatible polyelectrolyte multilayers (PEMs) consisting of the polycation chitosan (CHT) or poly(ethyleneimine) (PEI) and the polyanion sodium alginate (ALG) and their interactions with model‐protein human serum albumin (HSA). HSA‐adsorption data for PEI/ALG and CHT/ALG PEMs show the importance of the outermost polyelectrolyte (PEL) layer for protein interactions: CHT‐ or PEI‐terminated PEMs are highly attractive to HSA, while ALG‐terminated PEMs are repulsive, relevant for the generation of protein‐active or protein‐inert biomedical surfaces. The bound HSA is found to be located at the surface rather than the inner region of the PEM.