Toward Fully Synthetic Homogeneous β-Human Follicle-Stimulating Hormone (β-hFSH) with a Biantennary N-Linked Dodecasaccharide. Synthesis of β-hFSH with Chitobiose Units at the Natural Linkage Sites

Abstract
A highly convergent synthesis of the sialic acid-rich biantennary N-linked glycan found in human glycoprotein hormones and its use in the synthesis of a fragment derived from the β-domain of human Follicle-Stimulating Hormone (hFSH) are described. The synthesis highlights the use of the Sinaÿ radical glycosidation protocol for the simultaneous installation of both biantennary side-chains of the dodecasaccharide as well as the use of glycal chemistry to construct the tetrasaccharide core in an efficient manner. The synthetic glycan was used to prepare the glycosylated 20−27aa domain of the β-subunit of hFSH under a Lansbury aspartylation protocol. The proposed strategy for incorporating the prepared N-linked dodecasaccharide-containing 20−27aa domain into β-hFSH subunit was validated in the context of a model system, providing protected β-hFSH subunit functionalized with chitobiose at positions 7 and 24.

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