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The 1,3-diyne linker as a rigid "i,i+7" staple for α-helix stabilization: Stereochemistry at work
Steven Verlinden1, Niels Geudens2, Kevin Van Holsbeeck1,2
1Research Group of Organic Chemistry, Department of Chemistry and Department of Bioengineering Sciences, Faculty of Sciences and Bioengineering Sciences, Vrije Universiteit Brussel, Brussels, Belgium.
Abstract:
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.