Abstract

The production of cutting-edge materials, the development of novel medications, drug delivery systems, technological advancements, and biosynthesizing all depend on molecular building blocks. Proteins are required for the creation of intricate, well-organized structures, and coiled-coil protein domains are vital subunits for the oligomerization of protein complexes, gene expression, and the structural components of biological materials. The numerous interactions between a wide variety of amino acids make it difficult to assemble protein complexes with a particular shape. In the current study, we successfully designed and synthesized four different 32-residue peptides, each of which had two modified amino azide residues. These peptides were then used in solid-phase copper-catalyzed azide-alkyne cycloaddition (SP-CuAAC) click reactions to incorporate aryl aldehyde and acyl hydrazide functionalities into peptide oligomers. Although, results from LCMS indicate that individual peptides and click reaction product were successfully synthesized. Furthermore, we analyzed the orthogonality of peptide pairs by size exclusion chromatography (SEC) for self-assembly of paired coiled coil peptide and show successful association of dimeric coiled coils.

Date of publication

Spring 4-25-2023

Document Type

Thesis

Language

english

Persistent identifier

http://hdl.handle.net/10950/4177

Committee members

Sean C. Butler

Degree

Masters in chemistry

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