1-Aminocyclopentanecarboxylic acid (Ac5c) is a member of α,α-disubstituted α-amino acids and is known to stabilize the secondary structure of peptides containing Ac5c. We synthesized enantiomerically pure amino acids Ac5c3OAll having a 3-allyloxy group and two chiral centers at α and γ positions. These Ac5c3OAll were incorporated into L-leucine peptides sequence by solution-phase method. The formation of stapled side chain was performed by ring-closing metathesis between two allyloxy groups at the i and i+4 positions. We investigated secondary structure of synthesized peptides focused on the influence of stapled side chain. Peptides having cis-Hyp(All) and Aib instead of Ac5c3OAll and L-Leu, were also synthesized. These peptides were subjected to asymmetric epoxidation and Michael addition as an organocatalyst.

Conformational analysis of peptides having 1-aminocyclopentanecarboxylic acids with stapled side chain and their applications to organocatalysts

256th National Meeting (2018)

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