Self-assembling peptides and proteins regulate both function and dysfunction in the human body. Synthetic self-assembling peptides are often used to create biomaterials that mimic nature's materials due to their ability to form structurally diverse supramolecular assemblies through the collective combination of multiple noncovalent intramolecular forces. In many cases, the utility of mixing multiple peptides into a single supramolecular structure has been demonstrated for advantageous properties of the resultant material compared to materials composed of the individual components. The goal of the work presented in this thesis is to demonstrate new methodology and utility of novel synthetic biomaterials composed of multiple β-sheet peptides or Fmoc-phenylalanine amino acid derivatives. A new method of forming multicomponent biomaterials is presented with a split protein strategy employed for the formation of supramolecular fibrils composed of the self-assembling Ac-(FKFE)2-NH2 peptide that were decorated with multiple copies of functional proteins. A second novel material was investigated composed of "rippled β-sheets" that have mismatched amphipathic residues and hydrophobic interactions driving the self-assembly between Ac-(FKFE)2-NH2 and Ac-(VKVE)2-NH2 peptides. Lastly, novel cationic Fmoc-phenylalanine derivative hydrogel materials were investigated and their utility as drug delivery vehicles was demonstrated with in vivo delivery of non-steroidal anti-inflammatory drug, diclofenac, in mice.
|Advisor:||Nilsson, Bradley L.|
|Commitee:||Anthamatten, Mitchell, Dinnocenzo, Joseph P., Frontier, Alison J., White, Andrew D.|
|School:||University of Rochester|
|Department:||School of Arts and Sciences|
|School Location:||United States -- New York|
|Source:||DAI-B 80/09(E), Dissertation Abstracts International|
|Keywords:||Biomaterials, Drug delivery, Hydrogel, Multicomponent, Peptide, Supramolecular|
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