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The 1,3-diyne linker as a rigid "i,i+7" staple for alpha-helix stabilization: Stereochemistry at work

Tijdschriftbijdrage - Tijdschriftartikel

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.

Tijdschrift: J Pept Sci
ISSN: 1075-2617
Issue: 7
Volume: 25
Aantal pagina's: 9
Jaar van publicatie:2019
Trefwoorden:constrained peptides, Glaser-Hay coupling, helix stabilization, peptide stapling