Effects of protein inter-layers on cell-diamond FET characteristics
Language English Country England, Great Britain Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
20678916
DOI
10.1016/j.bios.2010.07.027
PII: S0956-5663(10)00402-1
Knihovny.cz E-resources
- MeSH
- Adsorption MeSH
- Biosensing Techniques instrumentation methods MeSH
- Cell Line MeSH
- Diamond chemistry MeSH
- Electrochemistry methods MeSH
- Transistors, Electronic * MeSH
- Ions MeSH
- Blood Proteins chemistry MeSH
- Humans MeSH
- Microscopy, Electron, Scanning MeSH
- Nanoparticles chemistry ultrastructure MeSH
- Surface Properties MeSH
- Solutions MeSH
- Cattle MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Cattle MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Diamond MeSH
- Ions MeSH
- Blood Proteins MeSH
- Solutions MeSH
Diamond is recognized as an attractive material for merging solid-state and biological systems. The advantage of diamond field-effect transistors (FET) is that they are chemically resistant, bio-compatible, and can operate without gate oxides. Solution-gated FETs based on H-terminated nanocrystalline diamond films exhibiting surface conductivity are employed here for studying effects of fetal bovine serum (FBS) proteins and osteoblastic SAOS-2 cells on diamond electronic properties. FBS proteins adsorbed on the diamond FETs permanently decrease diamond conductivity as reflected by the -45 mV shift of the FET transfer characteristics. Cell cultivation for 2 days results in a further shift by another -78 mV. We attribute it to a change of diamond material properties rather than purely to the field-effect. Increase in gate leakage currents (by a factor of 4) indicates that the FBS proteins also decrease the diamond-electrolyte electronic barrier induced by C-H surface dipoles. We propose a model where the proteins replace ions in the very vicinity of the H-terminated diamond surface.
References provided by Crossref.org
bOptimizing atomic force microscopy for characterization of diamond-protein interfaces