title: Mimics of peptide turn backbone and side-chain geometry by a general approach for modifying azabicyclo[5.3.0]alkanone amino acids.
abstract: Peptide mimics with constrained backbone and side-chain geometry are important tools for studying structure activity relationships of biologically active candidates. A general method for creating β-turn mimics possessing side-chain diversity has been developed featuring diastereoselective S(N)1 displacements of an iodide precursor. In particular, 6-iodo-pyrroloazepin-2-one amino ester 10 has served as a common precursor in reactions with a variety of alcohol, phenol, nitrate, and azide nucleophiles to provide an array of constrained peptide mimics.
authors.affiliation: Département de Chimie, Université de Montréal, Montréal, Québec, Canada.
authors.forename: Tanya A
authors.initials: TA
authors.lastname: Godina
authors.forename: William D
authors.initials: WD
authors.lastname: Lubell
mesh_terms: D000596:Amino Acids / Q000138:chemical synthesis* / Q000737:chemistry; D008968:Molecular Conformation; D018716:Molecular Mimicry; D010455:Peptides / Q000737:chemistry*; D013237:Stereoisomerism
chemical_list: D000596:Amino Acids; D010455:Peptides