title: β-Strand mimetic foldamers rigidified through dipolar repulsion.
abstract: Many therapeutically relevant protein-protein interactions contain hot-spot regions on secondary structural elements, which contribute disproportionately to binding enthalpy. Mimicry of such α-helical regions has met with considerable success, however the analogous approach for the β-strand has received less attention. Presented herein is a foldamer for strand mimicry in which dipolar repulsion is a central determinant of conformation. Computation as well as solution- and solid-phase data are consistent with an ensemble weighted almost exclusively in favor of the desired conformation.
authors.affiliation: Chemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA (UK) http://hamilton.chem.ox.ac.uk.
authors.forename: Elizabeth A
authors.initials: EA
authors.lastname: German
authors.forename: Jonathan E
authors.initials: JE
authors.lastname: Ross
authors.forename: Peter C
authors.initials: PC
authors.lastname: Knipe
authors.forename: Michaela F
authors.initials: MF
authors.lastname: Don
authors.forename: Sam
authors.initials: S
authors.lastname: Thompson
authors.forename: Andrew D
authors.initials: AD
authors.lastname: Hamilton
mesh_terms: D018360:Crystallography, X-Ray; D008958:Models, Molecular; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013816:Thermodynamics
chemical_list: D010455:Peptides
keywords: peptidomimetics; protein structures; protein-protein interactions; solid-state structures; synthetic methods