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Synthesis and solid state NMR characterization of novel peptide/silica hybrid materials.

Authors
  • Werner, Mayke1
  • Heil, Andreas1
  • Rothermel, Niels1
  • Breitzke, Hergen1
  • Groszewicz, Pedro Braga1
  • Thankamony, Aany Sofia1
  • Gutmann, Torsten2
  • Buntkowsky, Gerd3
  • 1 Eduard-Zintl-Institute of Inorganic and Physical Chemistry, Technical University of Darmstadt, Alarich-Weiss-Straße 4, D-64287 Darmstadt, Germany. , (Germany)
  • 2 Eduard-Zintl-Institute of Inorganic and Physical Chemistry, Technical University of Darmstadt, Alarich-Weiss-Straße 4, D-64287 Darmstadt, Germany. Electronic address: [email protected] , (Germany)
  • 3 Eduard-Zintl-Institute of Inorganic and Physical Chemistry, Technical University of Darmstadt, Alarich-Weiss-Straße 4, D-64287 Darmstadt, Germany. Electronic address: [email protected] , (Germany)
Type
Published Article
Journal
Solid state nuclear magnetic resonance
Publication Date
Nov 01, 2015
Volume
72
Pages
73–78
Identifiers
DOI: 10.1016/j.ssnmr.2015.09.008
PMID: 26411982
Source
Medline
Keywords
License
Unknown

Abstract

The successful synthesis and solid state NMR characterization of silica-based organic-inorganic hybrid materials is presented. For this, collagen-like peptides are immobilized on carboxylate functionalized mesoporous silica (COOH/SiOx) materials. A pre-activation of the silica material with TSTU (O-(N-Succinimidyl)-N,N,N',N'-tetramethyluronium tetrafluoroborate) is performed to enable a covalent binding of the peptides to the linker. The success of the covalent immobilization is indicated by the decrease of the (13)C CP-MAS NMR signal of the TSTU moiety. A qualitative distinction between covalently bound and adsorbed peptide is feasible by (15)N CP-MAS Dynamic Nuclear Polarization (DNP). The low-field shift of the (15)N signal of the peptide's N-terminus clearly identifies it as the binding site. The DNP enhancement allows the probing of natural abundance (15)N nuclei, rendering expensive labeling of peptides unnecessary.

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