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XPS and FT‐IR spectroscopy study of albumin adsorption on the surface of a π‐conjugated polymer film
Author(s) -
Iucci G.,
Polzonetti G.,
Infante G.,
Rossi L.
Publication year - 2004
Publication title -
surface and interface analysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.52
H-Index - 90
eISSN - 1096-9918
pISSN - 0142-2421
DOI - 10.1002/sia.1747
Subject(s) - x ray photoelectron spectroscopy , adsorption , chemistry , fourier transform infrared spectroscopy , bovine serum albumin , polymer , analytical chemistry (journal) , conjugated system , infrared spectroscopy , protein adsorption , spectroscopy , chromatography , chemical engineering , organic chemistry , physics , quantum mechanics , engineering
The interaction between thin films of polyphenylacetylene (PPA) and bovine serum albumin (BSA) dissolved in phosphate buffer solution (PBS) was studied by x‐ray photoelectron spectroscopy (XPS) and Fourier‐transform infrared spectroscopy (FT‐IR) performed in reflectance mode. PPA is a semiconducting π‐conjugated polymer consisting of a polyene backbone with phenyl pending groups, that has been used in the preparation of humidity sensors; therefore, we have tried to pre‐test PPA films for possible applications as biosensors. Thin films of PPA were incubated in buffered albumin solution (BSA/PBS) for increasing exposure times (24–96 hours). BSA adsorption on the PPA film surface takes place as demonstrated by the appearance of the N 1s signal and by the modifications in the C 1s core‐level signal in the XPS spectra of the samples treated with albumin solution; time‐dependent adsorption is also observed. Phosphate salts are co‐adsorbed on the PPA surface upon treatment with BSA/PBS solution. Albumin adsorption on the PPA surface was confirmed by FT‐IR measurements. Copyright © 2004 John Wiley & Sons, Ltd.

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