Uncovering a Latent Bioactive Interleukin-6 Glycoform.

ABSTRACT: A bioinspired semisynthesis of human-interleukin-6 bearing N-glycan at Asn143 (143glycosyl-IL-6) was performed by intentional glycosylation effects and protein folding chemistry for regioselective peptide-backbone activation. 143Glycosyl-IL-6 is a genetically coded cytokine, but isolation was difficult owing to a tiny amount. IL6-polypeptide (1-141-position) with an intentionally inserted cysteine at 142-position was expressed in E. coli. The expressed polypeptide was treated with a chemical folding process to make a specific helices bundle conformation through native two-disulfide bonds (43-49 and 72-82). Utilizing the successfully formed free-142-cysteine, sequential conversions using cyanylation of 142-cysteine, hydrazinolysis, and thioesterification created a long polypeptide (1-141)-t

SUBMITTER: Liu Y 

PROVIDER: S-EPMC11609956 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature