| Publication Type |
dissertation |
| School or College |
College of Pharmacy |
| Department |
Pharmaceutics & Pharmaceutical Chemistry |
| Author |
Xu, Chunyu |
| Title |
Protein-based hydrogels self-assembled from genetically engineered triblock containing coiled-coil domains |
| Date |
2006-08 |
| Description |
Protein-based biomaterials have great potential in biomedical applications due to their similar composition with biological organisms. Environment-sensitive hydrogels based on proteins can undergo sol-gel transition due to the conformational change of the proteins in response to external stimuli. The physical properties of these hydrogels can be tailored by modification of the protein structures. Two major hypotheses were made in this dissertation. One was that coiled-coil folding motifs could be a good candidate for physical crosslinking in protein-based hydrogels, and the other was that the conformational change of coiled-coils in response to external stimuli could mediate the sol-gel transition of the protein-based hydrogels. The first part established synthesis strategies of the coiled-coil containing proteins using a genetic engineering technique. An important observation was made that the fusion sequence on the proteins could influence the thermal stability of the proteins. In the second part of the research, the self-assembly of hydrogels from a series of triblock polypeptides containing coiled-coils was evaluated. It was found that the hydrogels had a porous interconnected network microstructure. The hydrogels responded to temperature and pH, which correlated to the temperature- and pH-triggered structural transition of the coiled-coil domains. In addition, the formation of hydrogels was reversible in the present or absence of guanidine hydrochloride (GdnHCl). The last part of the research attempted to explore the relationship between the structure of the protein polymers and the physical property of the hydrogels, and to investigate the parameters influencing the hydrogel formation and physical properties. Triblock and diblock polypeptides were designed to contain different lengths of coiled-coil domains. Tyrosine residues were incorporated at selected solvent-exposed positions in order to increase the hydrophobicity of the coiled-coil domains. The association of the coiled-coil domains was studied using the diblock polypeptides. Our results suggested that the hydrogel formation and physical properties may be influenced by other factors, such as the length of the central random coil segment, or selective inter-molecular association of tje cpil blocks. Environment-sensitive protein-based hydrogels in this dissertation represent a novel class of biomaterials. They can be used in a wide-range of biomedical applications in the future. |
| Type |
Text |
| Publisher |
University of Utah |
| Subject |
Hydrogels; triblock Polypeptides; Coiled-Coil; Self-Assembly; Pharmacology; Polymers; Materials Science |
| Subject MESH |
Peptides; Colloids; Protein Folding |
| Dissertation Institution |
University of Utah |
| Dissertation Name |
PhD |
| Language |
eng |
| Relation is Version of |
Digital reproduction of "Protein-based hydrogels self-assembled from genetically engineered triblock containing coiled-coil domains." Spencer S. Eccles Health Sciences Library. Print version of "Protein-based hydrogels self-assembled from genetically engineered triblock containing coiled-coil domains." available at J. Willard Marriott Library Special Collection. R117.5 2006 .X8. |
| Rights Management |
© Chunyu Xu. |
| Format Medium |
application/pdf |
| Format Extent |
2,312,711 bytes |
| Identifier |
undthes,5168 |
| Source |
Original: University of Utah Spencer S. Eccles Health Sciences Library (no longer available). |
| Master File Extent |
2,312,747 bytes |
| ARK |
ark:/87278/s61j9ckx |
| Setname |
ir_etd |
| ID |
190924 |
| Reference URL |
https://collections.lib.utah.edu/ark:/87278/s61j9ckx |
