title: A highly efficient type I β-turn mimetic simulating an Asx-Pro-turn-like structure.
abstract: Asx-Pro-turns have been identified with high frequency in protein structures nucleating type I β-turns. By bridging the amino acid side chain in position i with a nitrogen substituent in position i+2 by ring-closing olefin metathesis (RCM), peptide mimetics of type 1 could be developed. NMR based conformational investigations indicated a stable intramolecular H-bond constraining a U-turn conformation that was predicted to simulate a type I β-turn.
authors.affiliation: Department of Chemistry and Pharmacy, Emil Fischer Center, Friedrich Alexander University, Schuhstrasse 19, 91052 Erlangen, Germany.
authors.forename: Andrea
authors.initials: A
authors.lastname: Pinsker
authors.forename: Jürgen
authors.initials: J
authors.lastname: Einsiedel
authors.forename: Steffen
authors.initials: S
authors.lastname: Härterich
authors.forename: Reiner
authors.initials: R
authors.lastname: Waibel
authors.forename: Peter
authors.initials: P
authors.lastname: Gmeiner
mesh_terms: D040761:Biomimetic Materials / Q000138:chemical synthesis*; D004151:Dipeptides / Q000138:chemical synthesis*; D008958:Models, Molecular; D015394:Molecular Structure
chemical_list: D004151:Dipeptides