Materials Map

Discover the materials research landscape. Find experts, partners, networks.

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The Materials Map is an open tool for improving networking and interdisciplinary exchange within materials research. It enables cross-database search for cooperation and network partners and discovering of the research landscape.

The dashboard provides detailed information about the selected scientist, e.g. publications. The dashboard can be filtered and shows the relationship to co-authors in different diagrams. In addition, a link is provided to find contact information.

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The Materials Map is still under development. In its current state, it is only based on one single data source and, thus, incomplete and contains duplicates. We are working on incorporating new open data sources like ORCID to improve the quality and the timeliness of our data. We will update Materials Map as soon as possible and kindly ask for your patience.

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in Cooperation with on an Cooperation-Score of 37%

Topics

Publications (1/1 displayed)

  • 2008Specific peptide for functionalization of GaN - art. no. 699121citations

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Chart of shared publication
Larroque, C.
1 / 1 shared
Estephan, Elias
1 / 4 shared
Cloitre, Thierry
1 / 6 shared
Gergely, Csilla
1 / 9 shared
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2008

Co-Authors (by relevance)

  • Larroque, C.
  • Estephan, Elias
  • Cloitre, Thierry
  • Gergely, Csilla
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document

Specific peptide for functionalization of GaN - art. no. 699121

  • Larroque, C.
  • Estephan, Elias
  • Cloitre, Thierry
  • Cuisinier, F. J. G.
  • Gergely, Csilla
Abstract

Nanobiotechnology aims to exploit biomolecular recognition and self-assembly capabilities for integrating advanced materials into medicine and biology. However frequent problems are encountered at the interface of substrate-biological molecule, as the direct physical adsorption of biological molecules is dependent of unpredictable non-specific interactions with the surface, often causing their denaturation. Therefore, a proper functionalization of the substrate should avoid a loss of biological activity. In this work we address the functionalization of the semiconductor GaN (0001) for biosensing applications. The basic interest of using III-V class semiconductors is their good light emitting properties and a fair chemical stability that allows various applications of these materials. The technology chosen to elaborate GaN-specific peptides is the combinatorial phage-display method, a biological screening procedure based on affinity selection. An M13 bacteriophage library has been used to screen 10(10) different peptides against the GaN (0001) surface to finally isolate one specific peptide. The preferential attachment of the biotinylated selected peptide onto the GaN (0001), in close proximity to a surface of different chemical and structural composition has been demonstrated by fluorescence microscopy. Further physicochemical studies have been initiated to evaluate the semiconductor-peptide interface and understand the details in the specific recognition of peptides for semiconductor substrates. Fourier Transform Infrared spectroscopy in Attenuated Total Reflection mode (FTIR-ATR) has been employed to prove the presence of peptides on the surface. Our Atomic Force Microscopy (AFM) studies on the morphology of the GaN surface after functionalization revealed a total surface coverage by a very thin, homogeneous peptide layer. Due to its good biocompatibility, functionalized GaN devices might evolve in a new class of implantable biosensors for medical applications.

Topics
  • impedance spectroscopy
  • morphology
  • surface
  • atomic force microscopy
  • semiconductor
  • chemical stability
  • functionalization
  • Fourier transform infrared spectroscopy
  • self-assembly
  • biocompatibility
  • fluorescence microscopy