Our research is focused on developing an efficient way to synthesize peptide isosteres. Peptide isosteres are compounds that mimic the structure and size of peptides (or their larger counterparts, proteins), but have replaced the amide backbone with a different functional group. The amide backbone is responsible for the structure and binding of peptides and proteins and is readily hydrolyzed under physiological conditions. Peptide isosteres can thus be used to study the structure and binding of peptides or provide alternatives to peptide drugs that are not currently pharmacologically viable.The use of peptide isosteres is often limited by lengthy syntheses that are specific for a particular amino acid combination. We employ olefin cross metathesis to synthesize peptide isosteres, combining different carboxyl (C) and amino (N) termini. The focus of the current study is a more selective and efficent method to synthesize the C-termini utilizing a diasteroselective alkylation. Different chiral auxiliaries, alkylating agents and reaction conditions were examined to optimize the synthesis of this fragment.

Development of an efficient method for the synthesis of the C-terminal fragment of peptide isosteres

247th National Meeting (2014)

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