Stereochemistry of peptides containing 1‐aminocycloheptane‐1‐carboxylic acid (Ac7c)

Abstract
The crystal structures of four peptides incorporating l‐aminocycloheptane‐l‐carboxylic acid (Ac7c) are described. Boc‐Aib‐Ac7c‐NHMe and Boc‐Pro‐Ac7c‐Ala‐OMe adopt β‐turn conformations stabilized by an intramolecular 4 × 1 hydrogen bond, the former folding into a type‐I/III β‐turn and the latter into a type‐II β‐turn. In the dipeptide esters, Boc‐Aib‐Ac7c‐OMe and Boc‐Pro‐Ac7c‐OMe, the Ac7c and Aib residues adopt helical conformations, while the Pro residue remains semi‐extended in both the molecules of Boc‐Pro‐Ac7c‐OMe found in the asymmetric unit. The cycloheptane ring of Ac7c residues adopts a twist‐chair conformation in all the peptides studied. 1H‐NMR studies in CDCl3 and (CD3)2SO and IR studies in CDCl3, suggest that Boc‐Aib‐Ac7c‐NHMe and Boc‐Pro‐Ac7c‐Ala‐OMe maintain the β‐turn conformations in solution.