The development of novel, peptide based structures for tissue engineering materials has been widely researched, and its popularity can be attributed to advancements in technological analysis methods. Using principles based on protein structure and organization, this work describes the novel self-assembly of depsipeptides, which incorporate alternating esters within a native peptide backbone. Chapter 1 introduces and reviews peptide mimics for their utility for tissue engineering applications. Chapter 2 describes the methodology in synthesizing and characterization a depsipeptide library using both solution and solid phase methods. Chapter 3 discusses the effects of depsipeptide length, concentration, and sequence within a range of ionic concentrations and pH ranges on the self-assembly of depsipeptides into spherical nanostructures, fibers, or hydrogels. Chapter 4 describes proposed methods to increase the rate of gelation, followed by discussions of biocompatibility studies from other self-assembling peptide and modified-peptide systems in vitro and in vivo. The work described in this dissertation demonstrates that the synthesis and self-assembly of a depsipeptide family which alternates esters into a native peptide backbone does not disrupt the formation of higher order structures. This study illustrates the potential to synthesize a wide range of depsipeptides with variable side chains and hydrophobic character, as understanding these effects on self-assembly is imperative to the development of biomimetic materials for tissue engineering applications. / text
| Identifer | oai:union.ndltd.org:UTEXAS/oai:repositories.lib.utexas.edu:2152/25111 |
| Date | 11 July 2014 |
| Creators | Nguyen, Mary Minh Chau |
| Source Sets | University of Texas |
| Detected Language | English |
| Type | Thesis |
| Format | application/pdf |
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