Peptides are increasingly utilized as tools to investigate the role of specific protein-protein interactions, often times with the ultimate goal of developing a therapeutic agent.  Importantly, a well-defined secondary structure is typically required for the peptide to interact with either of the protein binding partners.  However, peptide fragments of proteins are structurally hampered, minimizing any binding affinity and demanding a chemical strategy to stabilize an expected secondary structure.   <br/>As the complexity of synthetic peptides increases, additional strategies that simplify peptide synthesis are also required.  Herein we present an optimization strategy for automating synthesis of helical peptides containing unnatural amino acids bearing an olefinic side chain functionality and constrained using on-resin ring-closing metathesis methods.<br/>

Stapled peptides: Optimizing automated synthesis and ring-closing metathesis

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.