Chemoenzymatic Synthesis of Asymmetrical Multi-Antennary N-Glycans to Dissect Glycan-Mediated Interactions between Human Sperm and Oocytes.

ABSTRACT: Complex N-glycans of glycoproteins of the zona pellucida (ZP) of human oocytes have been implicated in the binding of spermatozoa. The termini of these unusual bi-, tri-, and tetra-antennary N-glycans consist of the tetrasaccharide sialyl-Lewis^x (SLe^x ), which was previously identified as the minimal epitope for sperm binding. We describe here the chemoenzymatic synthesis of highly complex triantennary N-glycans derived from ZP carrying SLe^x moieties at the C-2 and C-2' arm and a sialyl-Lewis^x -Lewis^x (SLe^x -Le^x ) residue at the C-6 antenna and two closely related analogues. The compounds were examined for their ability to inhibit the interaction of human sperm to ZP. It was found that the SLe^x -Le

SUBMITTER: Chinoy ZS 

PROVIDER: S-EPMC5986622 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature