title: A modular synthesis of teraryl-based α-helix mimetics, part 1: Synthesis of core fragments with two electronically differentiated leaving groups.
abstract: Teraryl-based α-helix mimetics have proven to be useful compounds for the inhibition of protein-protein interactions (PPI). We have developed a modular and flexible approach for the synthesis of teraryl-based α-helix mimetics. Central to our strategy is the use of a benzene core unit featuring two leaving groups of differentiated reactivity in the Pd-catalyzed cross-coupling used for terphenyl assembly. With the halogen/diazonium route and the halogen/triflate route, two strategies have successfully been established. The synthesis of core building blocks with aliphatic (Ala, Val, Leu, Ile), aromatic (Phe), polar (Cys, Lys), hydrophilic (Ser, Gln), and acidic (Glu) amino acid side chains are reported.
authors.affiliation: Institute of Organic Chemistry, Graz University of Technology, Stremayrgasse 9, 8010 Graz, Austria.
authors.forename: Martin
authors.initials: M
authors.lastname: Peters
authors.forename: Melanie
authors.initials: M
authors.lastname: Trobe
authors.forename: Hao
authors.initials: H
authors.lastname: Tan
authors.forename: Rolf
authors.initials: R
authors.lastname: Kleineweischede
authors.forename: Rolf
authors.initials: R
authors.lastname: Breinbauer
mesh_terms: D000596:Amino Acids / Q000138:chemical synthesis* / Q000737:chemistry; D003432:Cross-Linking Reagents / Q000737:chemistry*; D006846:Hydrocarbons, Halogenated / Q000737:chemistry*; D015394:Molecular Structure; D010446:Peptide Fragments / Q000138:chemical synthesis* / Q000737:chemistry; D054730:Protein Interaction Domains and Motifs; D017433:Protein Structure, Secondary
chemical_list: D000596:Amino Acids; D003432:Cross-Linking Reagents; D006846:Hydrocarbons, Halogenated; D010446:Peptide Fragments