Vibrational and AFM studies of adsorption of glycine on DLC and silicon-doped DLC

A better understanding of protein adsorption onto surfaces of materials is required to control biocompatibility and bioactivity. Diamond-like carbon (DLC) is known to have excellent biocompatibility. Various samples of a-C:H and silicon-doped a-C:H thin films (Si-DLC) were deposited onto silicon sub...

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Veröffentlicht in:Journal of materials science 2012-02, Vol.47 (4), p.1729-1736
Hauptverfasser: Ahmed, M., Byrne, A. J., McLaughlin, J., Elhissi, A., Phoenix, D. A., Ahmed, W.
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Sprache:eng
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Zusammenfassung:A better understanding of protein adsorption onto surfaces of materials is required to control biocompatibility and bioactivity. Diamond-like carbon (DLC) is known to have excellent biocompatibility. Various samples of a-C:H and silicon-doped a-C:H thin films (Si-DLC) were deposited onto silicon substrates using plasma-enhanced chemical vapour deposition (PECVD). Subsequently, the adsorption of the simplest amino acid glycine onto the surfaces of the thin films was investigated to elucidate the mechanisms involved in protein adhesion. The physicochemical characteristics of the surfaces, before and after adsorption of glycine, were investigated using Raman spectroscopy and atomic force microscopy (AFM). The Raman study highlighted a slight decrease in the I D / I G ratio with increasing the silicon dopant levels. Following exposure to glycine solutions, the presence of bands at ~1735 and ~1200 cm −1 indicates that the adsorption of glycine onto the surfaces has taken place. Glycine was bound to the surfaces via both deprotonated carboxyl and protonated amino groups whilst, as the silicon content in the DLC film increased the adsorption of glycine decreased. AFM analysis showed that the surface roughness increased following exposure to glycine. These results show that at low silicon doping the adsorption of the amino acid was enhanced whilst increased doping levels led to a reduced adsorption compared to undoped DLC. Therefore, doping of DLC may provide an approach to control the protein adsorption.
ISSN:0022-2461
1573-4803
DOI:10.1007/s10853-011-5952-3