test Browse by Author Names Browse by Titles of Works Browse by Subjects of Works Browse by Issue Dates of Works

Advanced Search
& Collections
Issue Date   
Sign on to:   
Receive email
My Account
authorized users
Edit Profile   
About T-Space   

T-Space at The University of Toronto Libraries >
School of Graduate Studies - Theses >
Doctoral >

Please use this identifier to cite or link to this item: http://hdl.handle.net/1807/17247

Title: Self-assembly of Elatin-like Peptides: Studies by Single Molecule Imaging
Authors: Yang, Guocheng
Advisor: Yip, Christopher M.
Department: Chemical Engineering and Applied Chemistry
Issue Date: 26-Feb-2009
Abstract: 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.
URI: http://hdl.handle.net/1807/17247
Appears in Collections:Doctoral
Department of Chemical Engineering and Applied Chemistry - Doctoral theses

Files in This Item:

File Description SizeFormat
Yang_Guocheng_200811_PhD_thesis.pdf11.85 MBAdobe PDF

Items in T-Space are protected by copyright, with all rights reserved, unless otherwise indicated.