Understanding the basic mechanisms and dynamics that drive the assembly of molecules into functional structures is critically important in a diverse number of fields, ranging from materials science to drug delivery and biomaterials. In this work, we have focused on examining the self-assembly characteristics, both in solution and at surfaces, of a family of elastin-like peptides (EPs). In addition to directly observing the formation of ordered hexagonally arranged fibrillar EP structures on hydrophobic highly ordered pyrolytic graphite (HOPG), we have studied the dynamics of EP self-assembly process both within physically restricted domains using thermally etched HOPG, and in solution using detergent micelles. We have found that, at surfaces, EP fibril formation occurs via surface stabilization against the hydrophobic surface, while in solution, detergents inhibit EP aggregation at high temperatures and appear to enable the formation of an ordered crystalline structure at low temperatures. These model studies establish a framework for further investigations of peptide self-assembly and the role of hydrophobic interactions in controlling self-assembly.
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:OTU.1807/17247 |
| Date | 26 February 2009 |
| Creators | Yang, Guocheng |
| Contributors | Yip, Christopher M. |
| Source Sets | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
| Language | en_ca |
| Detected Language | English |
| Type | Thesis |
| Format | 12135488 bytes, application/pdf |
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