title: Enhancement of the helical content and stability induced in a linear oligopeptide by an i, i+4 intramolecularly double stapled, overlapping, bicyclic [31, 22, 5]-(E)ene motif.
abstract: Two consecutive i, i+4 intramolecular, side chain-to-side chain, macrocyclizations of different type carried out on a preformed, partially helical peptide result in a largely predominant, double stapled, overlapping, bicyclic [31,22,5]-(E)ene motif. A detailed ECD and NMR conformational study revealed a significant enhancement of the original helical content and stability, accompanied by an increase of the α-helix amount over that of the 3(10)-helix.
authors.affiliation: ICB, Padova Unit, CNR, Department of Chemistry, University of Padova, 35131 Padova, Italy.
authors.forename: Daniela
authors.initials: D
authors.lastname: Mazzier
authors.forename: Cristina
authors.initials: C
authors.lastname: Peggion
authors.forename: Claudio
authors.initials: C
authors.lastname: Toniolo
authors.forename: Alessandro
authors.initials: A
authors.lastname: Moretto
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D003500:Cyclization; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis* / Q000737:chemistry* / Q000302:isolation & purification; D017433:Protein Structure, Secondary; D066244:Proton Magnetic Resonance Spectroscopy
chemical_list: D009842:Oligopeptides
keywords: helical peptides; helix enhancements; macrocyclizations; spectroscopies; stapled peptide