Protein adsorption on thin films of carbon and carbon nitride monitored with in situ ellipsometry

Acta Biomater. 2011 Mar;7(3):1369-78. doi: 10.1016/j.actbio.2010.10.024. Epub 2010 Oct 25.

Abstract

Thin films of amorphous carbon and amorphous, graphitic and fullerene-like carbon nitride were deposited by reactive magnetron sputtering and optically characterized with spectroscopic ellipsometry. Complementary studies using scanning electron microscopy and atomic force microscopy were performed. The films were exposed to human serum albumin (HSA) and the adsorption was monitored in situ using dynamic ellipsometry. From the ellipsometric data the adsorbed amount of proteins was quantified in terms of surface mass density using de Feijter's model. The results indicate larger adsorption of proteins onto the amorphous films compared to the films with a more textured structure. Complementary studies with 125I-labeled HSA showed an apparent protein adsorption up to six times larger compared to the ellipsometry measurement. In addition, the four types of films were incubated in blood plasma followed by exposure to anti-fibrinogen, anti-HMWK or anti-C3c, revealing the materials' response to complement and contact activation. The amorphous and graphitic carbon nitride exhibit rather high immune activity compared to a titanium reference, whereas the amorphous carbon and the fullerene-like CNx show less immune complement deposition. Compared to the reference, all films exhibit indications of a stronger ability to initiate the intrinsic pathway of coagulation. Finally, the surfaces' bone-bonding ability was investigated by examination of their ability to form calcium phosphate crystals in a simulated body fluid, with a-CNx depositing most calcium phosphate after 21 days of incubation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adsorption
  • Carbon / chemistry*
  • Humans
  • Nitriles / chemistry*
  • Serum Albumin / chemistry*

Substances

  • Nitriles
  • Serum Albumin
  • cyanogen
  • Carbon