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