Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz
Gewählte Publikation:
SHR Neuro Krebs Kardio Lipid Stoffw Microb
Estephan, E; Larroque, C; Cuisinier, FJ; Bálint, Z; Gergely, C.
Tailoring GaN semiconductor surfaces with biomolecules.
J Phys Chem B. 2008; 112(29):8799-8805
Doi: 10.1021/jp804112y
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- Co-Autor*innen der Med Uni Graz
- Balint Zoltan
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- Abstract:
- Functionalization of semiconductors constitutes a crucial step in using these materials for various electronic, photonic, biomedical, and sensing applications. Within the various possible approaches, selection of material-binding biomolecules from a random biological library, based on the natural recognition of proteins or peptides toward specific material, offers many advantages, most notably biocompatibility. Here we report on the selective functionalization of GaN, an important semiconductor that has found broad uses in the past decade due to its efficient electroluminescence and pronounced chemical stability. A 12-mer peptide ("GaN_probe") with specific recognition for GaN has evolved. The subtle interplay of mostly nonpolar hydrophobic and some polar amino acidic residues defines the high affinity adhesion properties of the peptide. The interaction forces between the peptide and GaN are quantified, and the hydrophobic domain of the GaN_probe is identified as primordial for the binding specificity. These nanosized binding blocks are further used for controlled placement of biotin-streptavidin complexes on the GaN surface. Thus, the controlled grow of a new, patterned inorganic-organic hybrid material is achieved. Tailoring of GaN by biological molecules can lead to a new class of nanostructured semiconductor-based devices.
- Find related publications in this database (using NLM MeSH Indexing)
- Bacterial Proteins - analysis Bacterial Proteins - metabolism
- Binding Sites -
- Biotin - analogs and derivatives Biotin - analysis Biotin - metabolism
- Gallium - chemistry
- Hydrophobic and Hydrophilic Interactions -
- Microscopy, Atomic Force - methods
- Molecular Sequence Data -
- Nanostructures - chemistry
- Nanotechnology - methods
- Peptides - analysis Peptides - metabolism
- Semiconductors -
- Spectroscopy, Fourier Transform Infrared - methods
- Streptavidin - analysis Streptavidin - metabolism
- Surface Properties -
- Tissue Adhesions -