title: Conformational stability studies of a stapled hexa-β3-peptide library.
abstract: A library of 14-helical hexa β(3)-peptides was synthesized in order to determine the influence of sequence variation as well as staple size and location on conformational stability. From this study we show that appropriately stapled hexa-β(3)-peptides can allow for a number of variations without significant perturbation of the 14-helix.
authors.affiliation: School of Chemistry, Monash University, Clayton, VIC 3800, Australia.
authors.forename: Romila D
authors.initials: RD
authors.lastname: Gopalan
authors.forename: Mark P
authors.initials: MP
authors.lastname: Del Borgo
authors.forename: Ylva E
authors.initials: YE
authors.lastname: Bergman
authors.forename: Sharon
authors.initials: S
authors.lastname: Unabia
authors.forename: Roger J
authors.initials: RJ
authors.lastname: Mulder
authors.forename: Matthew C J
authors.initials: MC
authors.lastname: Wilce
authors.forename: Jacqueline A
authors.initials: JA
authors.lastname: Wilce
authors.forename: Marie-Isabel
authors.initials: MI
authors.lastname: Aguilar
authors.forename: Patrick
authors.initials: P
authors.lastname: Perlmutter
mesh_terms: D000475:Alkenes / Q000737:chemistry; D002942:Circular Dichroism; D008968:Molecular Conformation; D019151:Peptide Library; D055550:Protein Stability
chemical_list: D000475:Alkenes; D019151:Peptide Library