Get access

A Synthetic Approach to a Peptide α-Thioester from an Unprotected Peptide through Cleavage and Activation of a Specific Peptide Bond by N-Acetylguanidine

Authors

  • Dr. Ryo Okamoto,

    Corresponding author
    1. Department of Chemistry, Graduate School of Science, Osaka University, 1-1, Machikaneyama, Toyonaka, Osaka (Japan)
    • Department of Chemistry, Graduate School of Science, Osaka University, 1-1, Machikaneyama, Toyonaka, Osaka (Japan)
    Search for more papers by this author
  • Keiko Morooka,

    1. Department of Chemistry, Graduate School of Science, Osaka University, 1-1, Machikaneyama, Toyonaka, Osaka (Japan)
    Search for more papers by this author
  • Prof. Dr. Yasuhiro Kajihara

    Corresponding author
    1. Department of Chemistry, Graduate School of Science, Osaka University, 1-1, Machikaneyama, Toyonaka, Osaka (Japan)
    • Department of Chemistry, Graduate School of Science, Osaka University, 1-1, Machikaneyama, Toyonaka, Osaka (Japan)
    Search for more papers by this author

Abstract

original image

A different route to peptide α-thioesters through a new peptide-bond-cleavage method at a cysteine residue by S-thiocarbonylation and subsequent treatment with N-acetylguanidine is described (see scheme). The resultant peptidyl-N-acetylguanidine can be converted into the corresponding peptide α-thioester and is also usable as an alternative to a peptide α-thioester. This method allows efficient kinetically controlled ligation in the presence of thiols.

Ancillary