title: Design, synthesis and protein-targeting properties of thioether-linked hydrogen bond surrogate helices.
abstract: Appropriately-placed hydrogen bond surrogates have been demonstrated to efficiently nucleate helical conformations. Herein we describe an efficient method for the synthesis of thioether-based hydrogen bond surrogate (teHBS) helices. A teHBS helix is shown to adopt a stable conformation and target its cognate protein receptor with high affinity.
authors.affiliation: Department of Chemistry, New York University, New York, NY 10003, USA.
authors.forename: Andrew B
authors.initials: AB
authors.lastname: Mahon
authors.forename: Paramjit S
authors.initials: PS
authors.lastname: Arora
mesh_terms: D006860:Hydrogen Bonding; D017433:Protein Structure, Secondary; D013440:Sulfides / Q000737:chemistry*; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry*
chemical_list: D013440:Sulfides; D016159:Tumor Suppressor Protein p53