926661-76-9Relevant academic research and scientific papers
The use of a cysteinyl prolyl ester (CPE) autoactivating unit in peptide ligation reactions
Kawakami, Toru,Aimoto, Saburo
, p. 3871 - 3877 (2009)
A peptide containing a cysteinyl prolyl ester (CPE) moiety at the C-terminus (CPE peptide) is spontaneously transformed into a diketopiperazine thioester via an intramolecular N-S acyl shift reaction, followed by diketopiperazine formation. The CPE peptide can be ligated with a Cys-peptide in a one-pot procedure. The peptide diketopiperazine thioester can also be transformed into a peptide thioester by intermolecular thiol-thioester exchange with external thiol compounds such as sodium mercaptoethanesulfonate. Since CPE peptides can be prepared by standard Fmoc solid-phase synthesis, it is a versatile alternative to the peptide thioester, providing a flexible ligation strategy that promises to be useful in polypeptide synthesis.
A catalytic one-step synthesis of peptide thioacids: the synthesis of leuprorelin via iterative peptide-fragment coupling reactions
Matsumoto, Takuya,Sasamoto, Koki,Hirano, Ryo,Oisaki, Kounosuke,Kanai, Motomu
supporting information, p. 12222 - 12225 (2018/12/01)
A catalytic one-step synthesis of peptide thioacids was developed. The oxygen-sulfur atom exchange reaction converted the carboxy group at the C-terminus of the peptides into a thiocarboxy group with suppressed epimerization. This method was successfully applied to the synthesis of the peptide drug leuprorelin via an iterative fragment-coupling protocol.
3-Mercaptopropionic acid-mediated synthesis of peptide and protein thioesters
Kang, Jaskiranjit,Richardson, Jonathan P.,MacMillan, Derek
supporting information; experimental part, p. 407 - 409 (2009/05/06)
Peptides and proteins fragment sequence-specifically in the presence of 3-mercaptopropionic acid to afford thioesters which can be used in native chemical ligation reactions. The Royal Society of Chemistry.
