Details

Autor(en) / Beteiligte

• Zen, Federico
• Karanikolas, Vasilios D
• Behan, James A
• Andersson, Jenny
• Ciapetti, Guido
• Bradley, A. Louise
• Colavita, Paula E

Titel

Nanoplasmonic Sensing at the Carbon-Bio Interface: Study of Protein Adsorption at Graphitic and Hydrogenated Carbon Surfaces

Ist Teil von

• Langmuir, 2017-05, Vol.33 (17), p.4198-4206

Ort / Verlag

United States: American Chemical Society

Erscheinungsjahr

2017

Quelle

Alma/SFX Local Collection

Beschreibungen/Notizen

• Various forms of carbon are known to perform well as biomaterials in a variety of applications and an improved understanding of their interactions with biomolecules, cells, and tissues is of interest for improving and tailoring their performance. Nanoplasmonic sensing (NPS) has emerged as a powerful technique for studying the thermodynamics and kinetics of interfacial reactions. In this work, the in situ adsorption of two proteins, bovine serum albumin and fibrinogen, were studied at carbon surfaces with differing chemical and optical properties using nanoplasmonic sensors. The carbon material was deposited as a thin film onto NPS surfaces consisting of 100 nm Au nanodisks with a localized plasmon absorption peak in the visible region. Carbon films were fully characterized by X-ray photoelectron spectroscopy, atomic force microscopy, and spectroscopic ellipsometry. Two types of material were investigated: amorphous carbon (a-C), with high graphitic content and high optical absorptivity, and hydrogenated amorphous carbon (a-C:H), with low graphitic content and high optical transparency. The optical response of the Au/carbon NPS elements was modeled using the finite difference time domain (FDTD) method, yielding simulated analytical sensitivities that compare well with those observed experimentally at the two carbon surfaces. Protein adsorption was investigated on a-C and a-C:H, and the protein layer thicknesses were obtained from FDTD simulations of the expected response, yielding values in the 1.8–3.3 nm range. A comparison of the results at a-C and a-C:H indicates that in both cases fibrinogen layers are thicker than those formed by albumin by up to 80%.