Description
In this thesis the adsorption and self-assembly of spider silk mini spidroin peptide mimics is explored on fumed and Stöber silica nanoparticles. Dragline spider silk (major ampullate) fibers are comprised of two proteins, major ampullate spidroin 1 and 2 (MaSp1 and 2) that have highly repetitive core sequences consisting of certain consensus motifs, mainly poly(A), poly(GA), Poly(GGX) and GPGXX. This study is focused on synthesizing and characterizing the spider silk penta-alanine (A5) peptide mimic that comprises the region that forms the spider silk’s β-sheet core and hypothesized to impart spider silk its remarkable strength. The peptide is being synthesized using a CEM High Efficiency Solid Phase Peptide Synthesizer (HE-SPPS), purified using reverse phase High Performance Liquid Chromatography (HPLC), and structurally characterized with Matrix Assisted Laser Desorption Ionization Mass Spectrometry (MALDI-MS) and multinuclear, multidimensional solution Nuclear Magnetic Resonance (NMR) spectroscopy. In parallel, silica nanoparticles were synthesized via sol-gel methods and characterized using Transmission Electron Microscopy (TEM), Dynamic Light Scattering (DLS), Thermogravimetric Analysis (TGA), InfraRed (IR) Spectroscopy, and Solid State Nuclear Magnetic Resonance (SSNMR) spectroscopy. The spider silk peptide mimic is being used to functionalize the silica nanoparticles and develop spider silk-silica nanocomposite materials. The resulting peptide functionalized nanoparticles were investigated with NMR, TGA, TEM and DLS. This bio-nano composite is envisioned to have significant potential in hard tissue repair (bone and teeth) and drug delivery systems.
