292150-93-7Relevant articles and documents
Unmasking latent thioesters under hydrophobic-compatible conditions
Perkins, Wade S.,Davison, Ryan T.,Shelkey, Gregory B.,Lawson, Vernon E.,Hutton, Grace E.,Miller, Justin S.
, (2021)
Hydrophobic latent C-terminal thioesters were converted into thioesters, and were also coupled with cysteine in one-pot reactions, using conditions generally compatible with hydrophobic materials. The reaction conditions (ethanethiol and triethylamine in
Synthesis of Histidine-Containing Oligopeptides via Histidine-Promoted Peptide Ligation
Huang, Kai-Jin,Huang, Yi-Chen,Lin, Yuya A.
, p. 400 - 403 (2018/02/21)
Histidine-containing peptides are valuable therapeutic agents for a treatment of neurodegenerative diseases. However, the synthesis of histidine-containing peptides is not trivial due to the potential of imidazole sidechain of histidine to act as a nucleophile if unprotected. A peptide ligation method utilizing the imidazole sidechain of histidine has been developed. The key imidazolate intermediate that acts as an internal acyl transfer catalyst during ligation is generated by deprotonation. Transesterification with amino acids or peptides tethered with C-terminal thioester followed by N→N acyl shifts led to the final ligated products. A range of histidine-containing dipeptides could be synthesized in moderate to good yields via this method without protecting the imidazole sidechain. The protocol was further extended to tripeptide synthesis via a long-range N→N acyl transfer, and tetrapeptide synthesis.
Fmoc-based synthesis of peptide thioesters for native chemical ligation employing a tert -butyl thiol linker
Raz, Richard,Rademann, Joerg
supporting information; experimental part, p. 1606 - 1609 (2011/05/12)
tert-Butyl thioesters display an astonishing stability toward secondary amines in basic milieu, in contrast to other alkyl and aryl thioesters. Exploiting this enhanced stability, peptide thioesters were synthesized in a direct manner, applying a tert-butyl thiol linker for Fmoc-based solid-phase peptide synthesis.
