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Uncovering a Latent Bioactive Interleukin-6 Glycoform.

Yanbo Liu1, Yuta Maki1,2, Ryo Okamoto1,2

  • 1Department of Chemistry, Graduate School of Science, Osaka University, 1-1, Machikaneyama, Toyonaka, 560-0043, Japan.

Angewandte Chemie (International Ed. in English)
|August 5, 2024
PubMed
Summary

Researchers developed a novel semisynthesis for glycosylated human-interleukin-6 (143glycosyl-IL-6), overcoming isolation challenges. This bioinspired method yields a potent, folded cytokine with significant cell proliferation activity.

Keywords:
GlycoproteinInterleukin 6Protein aggregationProtein folding chemistryProtein synthesis

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Area of Science:

  • Biochemistry
  • Protein Engineering
  • Glycobiology

Background:

  • Human-interleukin-6 (IL-6) is a crucial cytokine, but its isolation in glycosylated forms is challenging.
  • Genetically coded glycosylation at Asn143 is difficult to achieve and study due to low yields.

Purpose of the Study:

  • To develop a bioinspired semisynthesis for producing human-interleukin-6 with N-glycan at Asn143 (143glycosyl-IL-6).
  • To enable the study of the bioactive conformation and function of this specific glycosylated cytokine.

Main Methods:

  • Semisynthesis involving regioselective peptide-backbone activation and protein folding chemistry.
  • Expression of IL6-polypeptide with a cysteine tag, chemical folding, and native chemical ligation.
  • Insertion of N-glycan tags for stabilization, followed by desulfurization and in vitro folding.

Main Results:

  • Successful semisynthesis of a whole 143glycosyl-IL-6 polypeptide (183 amino acids).
  • N-glycan tags enhanced the stability of intermediate polypeptide-thioesters.
  • The final folded 143glycosyl-IL-6 exhibited potent cell proliferation activity.

Conclusions:

  • The developed semisynthetic strategy enables efficient production of glycosylated IL-6.
  • The study provides insights into the bioactive conformation of latent 143glycosyl-IL-6 through integrated simulations and bioassays.