title: Helical α/β-depsipeptides with alternating residue types: conformational change from the 11-helix to the 14/15-helix.
abstract: Short α/β-peptides that consist of alternating l-α-amino acids and trans-2-aminocyclopentanecarboxylic acid are known to adopt both 11- and 14/15-helical conformations in solution. We report short α/β-depsipeptides containing (S)-lactic acid as the third residue from the N-terminus. The α/β-depsipeptide pentamers and heptamers adopt 14/15-helical conformations analogous to the α-helix in the crystal state and display 14/15-helical conformations predominantly in solution.
authors.affiliation: Department of Chemistry, Yonsei University, Seoul, 03722, Republic of Korea. sh-choi@yonsei.ac.kr.
authors.forename: Jaeyeon
authors.initials: J
authors.lastname: Lee
authors.forename: Geunhyeok
authors.initials: G
authors.lastname: Jang
authors.forename: Philjae
authors.initials: P
authors.lastname: Kang
authors.forename: Moon-Gun
authors.initials: MG
authors.lastname: Choi
authors.forename: Soo Hyuk
authors.initials: SH
authors.lastname: Choi
mesh_terms: D047630:Depsipeptides / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation
chemical_list: D047630:Depsipeptides