Optimizing the Semisynthesis towards glycosylated interferon-β-polypeptide by utilizing bacterial protein expression and chemical modification

Abstract

Synthesis of a sufficient amount of homogenous glycoprotein is of great interest because the natural glycoproteins show a considerable heterogeneity in oligosaccharide structures making the studies of glycan structure-function relationship...

Post-translational activation of the C-terminus of polypeptides for the synthesis of peptide thioesters and peptide thioester surrogates

“…Extending the idea of activation of a peptide bond by Cys side-chain modification, the Kajihara group also developed another expressed peptide thioesterification method based on S-cyanylation ( Figures 2B ) ( Kajihara et al, 2014 ; Chong et al, 2022 ). In this approach, the Xaa-Cys junction is activated by selective cyanylation of cysteine’s side chain using either 1-cyano-4-dimethylaminopyridium tetrafluoroborate (CDAP) or 2-nitro-5-thiocyanatobenzoic acid (NTCB), followed by the hydrazinolysis reaction under basic conditions to afford peptide hydrazide as a thioester surrogate.…”