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Glutathione adsorption from UHV to the liquid phase at various pH on gold and subsequent modification of protein interaction
Author(s) -
Vallée Anne,
Humblot Vincent,
Méthivier Christophe,
Pradier ClaireMarie
Publication year - 2008
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.2636
Subject(s) - chemistry , adsorption , glutathione , cationic polymerization , tripeptide , bovine serum albumin , monolayer , x ray photoelectron spectroscopy , ionic bonding , absorption (acoustics) , protein adsorption , inorganic chemistry , chromatography , organic chemistry , chemical engineering , peptide , ion , biochemistry , materials science , enzyme , engineering , composite material
This study is part of a project aiming at a better understanding of polypeptide and protein interactions with a metal surface. A tripeptide (the glutathione, or GSH) was deposited, under ultra high vacuum, on Au (111). From reflection–absorption infrared spectra (RAIRS), GSH was adsorbed in its zwiterrionic form which corresponds to the solid state one. GSH was also adsorbed on Au (111) surfaces from solutions at different pH values. These GSH so‐formed monolayers were then tested to anchor a well‐known protein, the bovine serum albumin (BSA); an effect of the structure and charge of the GSH layers on the protein adsorptions was made clear. The combination of XPS and polarisation‐modulation (PM)‐RAIRS results showed that the adsorbed GSH is in an identical form as that in solution (ionic state and conformation). When BSA is adsorbed from PBS solutions on the various layers of GSH the anionic or cationic nature of the GSH layer does not influence the adsorption of protein. On the other hand, adsorption of BSA in pure water is strongly favoured on cationic layers. Copyright © 2008 John Wiley & Sons, Ltd.