Peptide -- Silica Hybrid Networks

ORAL

Abstract

In this study, a bio-inspired route was used to fabricate scaffolds that display hierarchical organization of an inorganic layer around an organic self-assembled peptide fibril template. The 20 amino acid peptide used in this study intramolecular folds into a beta-hairpin conformation on addition of a desired solution stimulus. This intramolecular folding is followed by intermolecular self-assembly of the peptides into a three dimensional network of entangled fibrils rich in beta-sheet with a high density of lysine groups exposed on the fibril-surfaces. The lysine-rich surface chemistry was utilized to create a silica shell around the fibrils. The mineralization process of the fibrils results in a rigid, porous silica network that retains the microscale and nanoscale structure of the peptide fibril network. Structural characterization via Transmission Electron Microscopy, cryogenic-Scanning Electron Microscopy, mechanical characterization via oscillatory rheology, Small Angle X-ray and Neutron Scattering of the silicified hydrogels will be presented.

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Authors

  • Aysegul Altunbas

    Materials Science and Engineering, University of Delaware, UDEL

  • Nikhil Sharma

    UDEL, University of Delaware, Department of Materials Science and Engineering University of Delaware

  • Radhika Nagarkar

    UDEL, Department of Chemistry and Biochemistry, University of Delaware

  • Joel Schneider

    University of Delaware, Department of Chemistry and Biochemistry, University of Delaware

  • Darrin Pochan

    Department of Materials Science and Engineering and Delaware Biotechnology Institute, University of Delaware, Newark, DE 19716, USA, Materials Science and Engineering, University of Delaware, UDEL, Unviersity of Delaware, Department of Materials Science and Engineering University of Delaware, Department of Materials Science and Engineering and Delaware Biotechnology Institute, University of Delaware