In this work several self-assembling materials have been designed, synthesized, characterized and studied. These materials were based on synthetic peptides that were obtained through the solid phase peptide synthesis. First, collagen mimics were prepared through the polymerization of collagen-like peptides. Polymerization was done via native chemical ligation and yielded high molecular weight peptide polymers. The collagen-like structure of this polymers was confirmed by circular dichroism spectroscopy, size exclusion chromatography and transmission electron microscopy. Second, the internal structure of peptide amphiphiles was investigated. It was found that the formation of the hydrogen bonding network inside the nanofibers plays an important role in their self-assembly. In the absence of the hydrogen bonding a peptide amphiphile self-assembles into spherical micelles. Finally, the self-assembly of multidomain peptides was studied. The multidomain peptides were designed to combine several regions with different self-assembling motifs. The core region was made out of beta-sheet forming amino acids with the termini regions being either hydrophilic or electrostatically charged. When two of such peptides were mixed together it was found that their nanostructure, composed of fibers can be regulated and the fiber length can be controlled depending on the peptide molar ratio.
| Identifer | oai:union.ndltd.org:RICE/oai:scholarship.rice.edu:1911/20687 |
| Date | January 2007 |
| Creators | Paramonov, Sergey Evgenjevich |
| Contributors | Hartgerink, Jeffrey D. |
| Source Sets | Rice University |
| Language | English |
| Detected Language | English |
| Type | Thesis, Text |
| Format | 169 p., application/pdf |
Page generated in 0.0014 seconds