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All‐Thioamidated Homo‐α‐Peptides: Synthesis and Conformation
Author(s) -
Formaggio Fernando,
Crisma Marco,
Toniolo Claudio,
Peggion Cristina
Publication year - 2013
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/ejoc.201300050
Subject(s) - chemistry , thioamide , peptidomimetic , oligopeptide , peptide , stereochemistry , amino acid , nuclear magnetic resonance spectroscopy , context (archaeology) , peptide bond , combinatorial chemistry , biochemistry , paleontology , biology
Replacement of a peptide bond with its thioamide surrogate is a classical method for the generation of a peptidomimetic with altered spectroscopic, conformational, physicochemical, and biological properties. In this context, we synthesized short series of terminally protected homo‐α‐oligopeptides based on the α‐amino acids Gly, Ala, and Nle, as well as their corresponding fully thioamidated analogues. For the first time, the preparation of the latter compounds was achieved in single‐step fashion through direct thionation of their oxygenated precursors. Using X‐ray diffraction analysis and NMR spectroscopy we were also able to confirm that the thioamidated α‐amino acid residues can easily adopt either folded or fully extended conformations.