We present a spectroscopic study of the structure of two peptides deposited on Au 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 b-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.
Peptides adsorption on TiO2 and Au: molecular organization investigated by NEXAFS, XPS and IR
DETTIN, MONICA;DI BELLO, CARLO;
2007
Abstract
We present a spectroscopic study of the structure of two peptides deposited on Au 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 b-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.
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