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Okamoto R, Iritani K, Amazaki Y, et al. Semisynthesis of a Homogeneous Glycoprotein Using Chemical Transformation of Peptides to Thioester Surrogates. J Org Chem. 2021;87(1):114-124doi: 10.1021/acs.joc.1c02031.
Okamoto, R., Iritani, K., Amazaki, Y., Zhao, D., Chandrashekar, C., Maki, Y., Kanemitsu, Y., Kaino, T., & Kajihara, Y. (2022). Semisynthesis of a Homogeneous Glycoprotein Using Chemical Transformation of Peptides to Thioester Surrogates. The Journal of organic chemistry, 87(1), 114-124. https://doi.org/10.1021/acs.joc.1c02031
Okamoto, Ryo, et al. "Semisynthesis of a Homogeneous Glycoprotein Using Chemical Transformation of Peptides to Thioester Surrogates." The Journal of organic chemistry vol. 87,1 (2022): 114-124. doi: https://doi.org/10.1021/acs.joc.1c02031
Okamoto R, Iritani K, Amazaki Y, Zhao D, Chandrashekar C, Maki Y, Kanemitsu Y, Kaino T, Kajihara Y. Semisynthesis of a Homogeneous Glycoprotein Using Chemical Transformation of Peptides to Thioester Surrogates. J Org Chem. 2022 Jan 07;87(1):114-124. doi: 10.1021/acs.joc.1c02031. Epub 2021 Dec 10. PMID: 34889597.
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J Org Chem. 2022 Jan 07;87(1):114-124. doi: 10.1021/acs.joc.1c02031. Epub 2021 Dec 10.

Semisynthesis of a Homogeneous Glycoprotein Using Chemical Transformation of Peptides to Thioester Surrogates.

The Journal of organic chemistry

Ryo Okamoto, Kento Iritani, Yoko Amazaki, Donglin Zhao, Chaitra Chandrashekar, Yuta Maki, Yurie Kanemitsu, Tomoka Kaino, Yasuhiro Kajihara

Affiliations

  1. Department of Chemistry, Graduate School of Science, Osaka University, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan.
  2. Project Research Center for Fundamental Sciences, Graduate School of Science, Osaka University, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan.

PMID: 34889597 DOI: 10.1021/acs.joc.1c02031

Abstract

Semisynthesis using recombinant polypeptides as building blocks is a powerful approach for the preparation of proteins with a variety of modifications such as glycosylation. The activation of the C terminus of recombinant peptides is a key step for coupling peptide building blocks and preparing a full-length polypeptide of a target protein. This article reports two chemical approaches for transformation of the C terminus of recombinant polypeptides to thioester surrogates. The first approach relies on efficient substitution of the C-terminal Cys residue with bis(2-sulfanylethyl)amine (SEA) to yield peptide-thioester surrogates. The second approach employs a native tripeptide, cysteinyl-glycyl-cysteine (CGC), to yield peptide-thioesters via a process mediated by a thioester surrogate. Both chemical transformation methods employ native peptide sequences and were thereby successfully applied to recombinant polypeptides. As a consequence, we succeeded in the semisynthesis of a glycosylated form of inducible T cell costimulator (ICOS) for the first time.

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