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A NEXAFS and XPS study of the adsorption of self‐assembling peptides on TiO 2 : the influence of the side chains
Author(s) -
Iucci Giovanna,
Battocchio Chiara,
Dettin Monica,
Gambaretto Roberta,
Polzonetti Giovanni
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.2717
Subject(s) - xanes , x ray photoelectron spectroscopy , fourier transform infrared spectroscopy , adsorption , chemistry , aqueous solution , side chain , absorption (acoustics) , peptide , crystallography , spectroscopy , chemical engineering , organic chemistry , materials science , polymer , biochemistry , physics , quantum mechanics , engineering , composite material
Peptides consisting of an alternation of hydrophobic and hydrophilic (positively and negatively charged) amino acids can generate extended ordered structures by self‐assembling (SA) from aqueous solutions. In this paper we present XPS, near‐edge X‐ray absorption fine structure (NEXAFS) and Fourier transform infrared (FTIR) investigations on a series of SA peptides with the aim of determining the effect of side‐chain length on molecular arrangement and orientation. Peptides were immobilised on the surface of titanium, a well‐known biocompatible material, or deposited as thick films on inert gold surfaces. FTIR analysis yields information on the backbone conformation. XPS spectroscopy was used to investigate the peptide adsorption on the TiO 2 surface. The orientation of the peptide chains was investigated by angular‐dependent NEXAFS. Copyright © 2008 John Wiley & Sons, Ltd.