A synthetic approach to a peptide α-thioester from an unprotected peptide through cleavage and activation of a specific peptide bond by N-acetylguanidine.

@article{Okamoto2012ASA,
  title={A synthetic approach to a peptide α-thioester from an unprotected peptide through cleavage and activation of a specific peptide bond by N-acetylguanidine.},
  author={Ryo Okamoto and Keiko Morooka and Yasuhiro Kajihara},
  journal={Angewandte Chemie},
  year={2012},
  volume={51 1},
  pages={
          191-6
        }
}
In modern procedures for total chemical protein synthesis, the concept of chemical ligation plays an essential role in the assembly of target protein polypeptide chains. The peptide a-thioester is the key component for chemical ligation such as native chemical ligation (NCL), direct segment coupling methods, or traceless Staudinger ligation. Thus, substantial effort has been expended on the establishment of peptide-athioester synthesis based on conventional Boc or Fmoc solidphase peptide… CONTINUE READING
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