title: Peptoid atropisomers.
abstract: We report the isolation of N-aryl peptoid oligomers that adopt chiral folds, despite the absence of chiral centers. Peptoid monomers incorporating ortho-substituted N-aryl side chains are identified that exhibit axial chirality. We observe significant energy barriers to rotation about the stereogenic carbon-nitrogen bond, allowing chromatographic purification of stable atropisomeric forms. We study the atropisomerism of N-aryl peptoid oligomers by computational modeling, NMR, X-ray crystallography, dynamic HPLC, and circular dichroism. The results demonstrate a new approach to promote the conformational ordering of this important class of foldamer compounds.
authors.affiliation: Department of Chemistry, New York University, New York, New York 10003, USA.
authors.forename: Bishwajit
authors.initials: B
authors.lastname: Paul
authors.forename: Glenn L
authors.initials: GL
authors.lastname: Butterfoss
authors.forename: Mikki G
authors.initials: MG
authors.lastname: Boswell
authors.forename: P Douglas
authors.initials: PD
authors.lastname: Renfrew
authors.forename: Fanny G
authors.initials: FG
authors.lastname: Yeung
authors.forename: Neel H
authors.initials: NH
authors.lastname: Shah
authors.forename: Christian
authors.initials: C
authors.lastname: Wolf
authors.forename: Richard
authors.initials: R
authors.lastname: Bonneau
authors.forename: Kent
authors.initials: K
authors.lastname: Kirshenbaum
mesh_terms: D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D018360:Crystallography, X-Ray; D019281:Dimerization; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D034444:Peptoids / Q000737:chemistry*; D011487:Protein Conformation; D012399:Rotation; D013237:Stereoisomerism
chemical_list: D034444:Peptoids