Document Type

Honors Project On-Campus Access Only


Proteins have desirable functionality in applications other than that of their biological origin, such as enzymes, which may be applied to industry. However, proteins are often unstable outside of their natural environments, making them difficult to use in an efficient manner. One way to relieve this is the use of protein-mimetics, which can have increased stability outside biological environments while also retaining functionality. In this thesis, I approached protein-mimetics from two different angles. The first mimic was a structural peptidomimetic that was synthesized using a pre-monomer approach. This is a solid phase synthetic strategy that separates the backbone elongation from the addition of the side chain functionality. The key thiol-ene coupling reaction for this approach was optimized to result in over 95% reaction conversion. The second type of mimic focused on catalytic activity of short peptide catalysts for ester hydrolysis and investigating the role of secondary structure on that activity. We found that the secondary structure’s role is dependent on the design scaffold through analysis of two separate β-hairpin scaffolds.



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