title: Stabilization of 11/9-helical α/β-peptide foldamers in protic solvents.
abstract: α/β-Peptides with alternating α-amino acid and cis-2-aminocyclohexanecarboxylic acid (cis-ACHC) residues adopt 11/9-helical conformations, the folding propensity of which decreases as the solvent polarity increases. We report a new cis-ACHC analogue, cis-2-amino-cis-4-methylcyclohexanecarboxylic acid, which significantly stabilizes the 11/9-helix propensity in protic solvents.
authors.affiliation: Department of Chemistry, Yonsei University, Seoul, 03722, Republic of Korea. sh-choi@yonsei.ac.kr.
authors.forename: Mihye
authors.initials: M
authors.lastname: Lee
authors.forename: Jihyun
authors.initials: J
authors.lastname: Shim
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: D000596:Amino Acids / Q000737:chemistry; D003509:Cyclohexanecarboxylic Acids / Q000737:chemistry; D003514:Cyclohexylamines / Q000737:chemistry; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D000072756:Protein Conformation, alpha-Helical; D017510:Protein Folding / Q000187:drug effects*; D055550:Protein Stability / Q000187:drug effects; D012997:Solvents / Q000737:chemistry / Q000494:pharmacology*
chemical_list: D000596:Amino Acids; D003509:Cyclohexanecarboxylic Acids; D003514:Cyclohexylamines; D010455:Peptides; D012997:Solvents; C103271:2-aminocyclohexanecarboxylic acid