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, accompained by an increase of the alpha-helix amount over that of the 3(10)-helix.

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

Toniolo C;Moretto A
2014

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, accompained by an increase of the alpha-helix amount over that of the 3(10)-helix.
2014
Istituto di Chimica Biomolecolare - ICB - Sede Pozzuoli
helical peptides
helix enhancements
macrocyclizations
spectroscopies
stapled peptide
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/227836
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