title: Peptide N-Amination Supports β-Sheet Conformations.
abstract: The conformational heterogeneity of backbone N-substituted peptides limits their ability to adopt stable secondary structures. Herein, we describe a practical synthesis of backbone aminated peptides that readily adopt β-sheet folds. Data derived from model N-amino peptides suggest that extended conformations are stabilized through cooperative steric, electrostatic, and hydrogen-bonding interactions.
authors.affiliation: Department of Chemistry, University of South Florida, 4202 E. Fowler Avenue, Tampa, FL, 33620, USA.
authors.forename: Matthew P
authors.initials: MP
authors.lastname: Sarnowski
authors.affiliation: Department of Chemistry, University of South Florida, 4202 E. Fowler Avenue, Tampa, FL, 33620, USA.
authors.forename: Chang Won
authors.initials: CW
authors.lastname: Kang
authors.affiliation: Department of Chemistry, University of South Florida, 4202 E. Fowler Avenue, Tampa, FL, 33620, USA.
authors.forename: Yassin M
authors.initials: YM
authors.lastname: Elbatrawi
authors.affiliation: Department of Chemistry, University of South Florida, 4202 E. Fowler Avenue, Tampa, FL, 33620, USA.
authors.forename: Lukasz
authors.initials: L
authors.lastname: Wojtas
authors.affiliation: Department of Chemistry, University of South Florida, 4202 E. Fowler Avenue, Tampa, FL, 33620, USA.
authors.forename: Juan R
authors.initials: JR
authors.lastname: Del Valle
keywords: foldamers; peptidomimetics; secondary structures; β-hairpins; β-strands