All most all eukaryotic cell surface and secreted proteins are modified by covalently-linked glycans which are essential mediators of biological processes such as protein folding, cell signaling, fertilization, embryogenesis, and the proliferation of cells and their organization into specific tissues. Overwhelming data supports the relevance of glycosylation in pathogen recognition, inflammation, innate immune responses, the development of autoimmune diseases, and cancer.  It has, however, been difficult to explore biological properties of individual glycans because these bio-molecules are not readily available. To address this challenge, we have developed chemo-enzymatic methodologies that make it possible to prepare large collections of highly complex asymmetrically substituted glycans. The methodology has been used to prepare multi-antennary oligosaccharides that can inhibit binding of spermatozoan to the <i>zona pellucida</i> of human oocytes. Furthermore, we have synthesized a series of complex oligosaccharides that were printed as microarrays and screened for binding of influenza-virus hemagglutinins. It was found that recognition is modulated by presentation of minimal epitopes in the context of complex <i>N</i>-glycans. We have also developed chemo-enzymatic methodologies to prepare of human milk oligosaccharides (HMOs) that were employed to identify compounds that function as decoys for viral and bacteria adhesion.

Glycan complexity and biological recognition

256th National Meeting (2018)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.