We present a spectroscopic study of the structure of two peptides deposited on An and TiO2: - PeptA, (EAK16-RGD) bringing the adhesive RGD sequence linked to EAK16; - PeptB, having RGD linked to a "scrambled" sequence of the EAK16 peptide. Previously reported NEXAFS investigations on thin films of the self-assembling peptide EAK16 deposited on Au and TiO2, revealed molecular order and orientation for both substrates. IR spectra show a beta-sheet conformation for PeptA and a random structure for PeptB. Angular-dependent NEXAFS measurements reveal an ordered structure with preferential molecular orientation only for PeptA. XPS analysis indicates that PeptA is adsorbed on TiO2 in a larger amount than PeptB.
Iucci, G., Battocchio, C., Dettin, M., Gambaretto, R., DI BELLO, C., Borgatti, F., et al. (2007). Peptides adsorption on TiO2 and Au: Molecular organization investigated by NEXAFS, XPS and IR. SURFACE SCIENCE, 601, 3843-3849 [10.1016/j.susc.2007.04.024].
Peptides adsorption on TiO2 and Au: Molecular organization investigated by NEXAFS, XPS and IR
IUCCI, GIOVANNA;BATTOCCHIO, CHIARA;
2007-01-01
Abstract
We present a spectroscopic study of the structure of two peptides deposited on An and TiO2: - PeptA, (EAK16-RGD) bringing the adhesive RGD sequence linked to EAK16; - PeptB, having RGD linked to a "scrambled" sequence of the EAK16 peptide. Previously reported NEXAFS investigations on thin films of the self-assembling peptide EAK16 deposited on Au and TiO2, revealed molecular order and orientation for both substrates. IR spectra show a beta-sheet conformation for PeptA and a random structure for PeptB. Angular-dependent NEXAFS measurements reveal an ordered structure with preferential molecular orientation only for PeptA. XPS analysis indicates that PeptA is adsorbed on TiO2 in a larger amount than PeptB.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
