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The 1,3‐diyne linker as a rigid “ i , i +7” staple for α‐helix stabilization: Stereochemistry at work
Author(s) -
Verlinden Steven,
Geudens Niels,
Van holsbeeck Kevin,
Mannes Morgane,
Martins José C.,
Verniest Guido,
Ballet Steven
Publication year - 2019
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.3194
Subject(s) - linker , chemistry , stereochemistry , peptide , helix (gastropod) , crystallography , biochemistry , biology , computer science , ecology , snail , operating system
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.