| Publication Type |
dissertation |
| School or College |
College of Pharmacy |
| Department |
Pharmaceutics & Pharmaceutical Chemistry |
| Author |
Ramachandran, Sivakumar |
| Contributor |
Trewhella, Jill; Taraban, Marc; Carrier, Stacey L.; Flinders, Kurt |
| Title |
Design and characterization of peptide-based biomaterials |
| Date |
2007-05 |
| Description |
The main objective of this dissertation is to lay out the design principles involved in assembling stimuli-sensitive, peptide-based biomaterials that has potential for various biomedical applications like tissue engineering and drug delivery. Supramolecular systems, which enable one to assemble novel materials from molecular level, have fascinated researchers in many disciplines. Inspired by such systems, a set of mutually complementary, self-repulsive oligopeptide modules (with alternating polar-apolar amino acid sequence) were designed to gain better control and wide range of tunability over the assembling process. These peptide modules (at 0.25 wt% in aqueous buffer) assembled into a hydrogel network with change in pH/ionic strength (self-assembly) and upon mixing the two mutually-complementary peptide modules (co-assembly). Mixing induced hydrogels are particularly attractive as they can be easily assembled by simple mixing of peptide solutions prior to application. Another advantage of mixing-induced gelation is that it preserves the pH and ionic strength of the original peptide solutions. Circular dichroism spectroscopy of individual decapeptide solutions revealed their random coil conformation. Transmission electron microscopy images showed the nanofibrillar network structure of the hydrogel. Dynamic rheological characterization revealed its high elasticity and shear-thinning nature. Furthermore, the co-assembled hydrogel was capable of rapid recoveries from repeated shear-induced breakdowns, a property desirable for designing injectable biomaterials. A systematic variation of the neutral amino acids in the sequence revealed some of the design principles for this class of biomaterials. First, viscoelastic properties of the hydrogels can be tuned through adjusting the hydrophobicity of the neutral amino acids. Second, the ?-sheet propensity of the neutral amino acid residue in the peptides is critical for hydrogelation. The compatibility of these hydrogels with entrapped biomolecules (molecular biocompatibility) was confirmed using high-resolution, <super>1 |
| Type |
Text |
| Publisher |
University of Utah |
| Subject |
Biomedical Materials; Biocompatibility; Theraputic Use |
| Subject MESH |
Peptides; Biomedical Engineering; Hydrogels |
| Dissertation Institution |
University of Utah |
| Dissertation Name |
PhD |
| Language |
eng |
| Relation is Version of |
Digital reproduction of "Design and characterization of peptide-based biomaterials". Spencer S. Eccles Health Sciences Library. Print version of "Design and characterization of peptide-based biomaterials". available at J. Willard Marriott Library Special Collection. R117.5 2007 .R34. |
| Rights Management |
© Sivakumer Ramachandran. |
| Format Medium |
application/pdf |
| Format Extent |
1,462,514 bytes |
| Identifier |
undthes,4586 |
| Source |
Original: University of Utah Spencer S. Eccles Health Sciences Library (no longer available). |
| Funding/Fellowship |
National Institutes of Health under grant RB004416, Novartis Fellowship, Gratuate research Fellowship (Universtiy of Utah), and travel award for GPRN 2004 (Universtiy of Utah). |
| Master File Extent |
1,462,558 bytes |
| ARK |
ark:/87278/s6s184cm |
| Setname |
ir_etd |
| ID |
191700 |
| Reference URL |
https://collections.lib.utah.edu/ark:/87278/s6s184cm |
