title: Evaluation of a cyclopentane-based γ-amino acid for the ability to promote α/γ-peptide secondary structure.
abstract: We report the asymmetric synthesis of the γ-amino acid (1R,2R)-2-aminomethyl-1-cyclopentane carboxylic acid (AMCP) and an evaluation of this residue's potential to promote secondary structure in α/γ-peptides. Simulated annealing calculations using NMR-derived distance restraints obtained for α/γ-peptides in chloroform reveal that AMCP-containing oligomers are conformationally flexible. However, additional evidence suggests that an internally hydrogen-bonded helical conformation is partially populated in solution. From these data, we propose characteristic NOE patterns for the formation of the α/γ-peptide 12/10-helix and discuss the apparent conformational frustration of AMCP-containing oligomers.
authors.affiliation: Department of Chemistry, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States.
authors.forename: Michael W
authors.initials: MW
authors.lastname: Giuliano
authors.forename: Stacy J
authors.initials: SJ
authors.lastname: Maynard
authors.forename: Aaron M
authors.initials: AM
authors.lastname: Almeida
authors.forename: Andrew G
authors.initials: AG
authors.lastname: Reidenbach
authors.forename: Li
authors.initials: L
authors.lastname: Guo
authors.forename: Emily C
authors.initials: EC
authors.lastname: Ulrich
authors.forename: Ilia A
authors.initials: IA
authors.lastname: Guzei
authors.forename: Samuel H
authors.initials: SH
authors.lastname: Gellman
mesh_terms: D000596:Amino Acids / Q000138:chemical synthesis / Q000737:chemistry*; D003517:Cyclopentanes / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry*
chemical_list: D000596:Amino Acids; D003517:Cyclopentanes; D010455:Peptides