Characterization of peptide adsorption on InAs using X-ray photoelectron spectroscopy.

The well-defined structure and high stability of peptides make them attractive biotemplates for low-temperature synthesis of semiconductor nanocrystals. Adsorbed peptide monolayers could also potentially passivate semiconductors by preventing regrowth of the oxide layer. In this work, the adsorption and passivation capabilities of different collagen-binding peptides on InAs surfaces were analyzed by X-ray photoelectron spectroscopy (XPS). Before peptide functionalization, Br(2)- and HCl-based etches were used to remove the native oxide layer on the InAs surfaces. The presence of the N 1s peak for peptide-functionalized samples confirms the adsorption of peptides onto the etched InAs surfaces. Calculated coverages were similar for all peptide sequences and ranged from ∼20 to 40% of a monolayer using the deconvoluted C 1s spectra and from ∼2 to 5% for the N 1s spectra. The passivation ability of the peptides was analyzed by comparing the ratios of the oxide components to the nonoxide components in the XPS spectra. The thickness of the oxide layer was also approximated by accounting for the attenuation of the substrate photoelectrons through the oxide layer. We find that the oxide layer regrowth still occurs after peptide functionalization. However, the oxide layer thicknesses for peptide-functionalized samples do not reach as received levels, indicating that the peptides do have some passivation ability on InAs.