Short alphahelical peptide sequences were stabilized through Glaser-Hay couplings of propargylated l- and/or d-serine residues at positions i and i+7. NMR analysis confirmed a full stabilization of the helical structure when a d-Ser (i), l-Ser (i+7) combination was applied. In case two l-Ser residues were involved in the cyclization, the helical conformation is disrupted outside the peptide's macrocycle.

Original languageEnglish
Number of pages9
JournalJournal of Peptide Science
Issue number7
Publication statusPublished - Jul 2019

    Research areas

  • constrained peptides, Glaser-Hay coupling, helix stabilization, peptide stapling

ID: 46776674