DOI

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
Volume25
Issue number7
DOIs
Publication statusPublished - Jul 2019

    Research areas

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

ID: 46776674