Topological Study of the Structures of Heterochiral Peptides Containing Equal Amounts of l‑Leu and d‑Leu

We designed and synthesized two dodecapeptides,
Boc-(l-Leu-l-Leu-Aib-d-Leu-d-Leu-Aib)2-OMe (5) and Boc-l-Leu-l-Leu-Aib-(d-Leu-d-Leu-Aib)2-l-Leu-l-Leu-Aib-OMe (6), that contain equal amounts of l-Leu, d-Leu, and achiral Aib residues. The conformations
of peptides 5 and 6 in the crystalline state
were studied using X-ray crystallographic analysis. Peptide 5 formed a left-handed (M) α-helical
structure, whereas peptide 6 was composed of a combination
of fused (M) α-helical and right-handed (P) 310-helical structures. In solution, roughly
equivalent amounts of (P) and (M) helices were present in 5, whereas the (M) α-helix was present in 6 as its dominant conformation.