Protein glycoconjugates, protein products modified with intricate glycan post-translational modifications, are often considered untamable biomolecules. A single glycoconjugate can exist in thousands of heterogeneous unique protein glycoforms in living cells, resulting in innumerable possible interactions and functions. Despite the structural diversity of glycoconjugates and the complexities of their interactions, there is information encoded in these molecular messages, such that they play key roles in orchestrating physiology and disease. However, current approaches to describe protein glycoconjugates and their interactions are limited, restraining our understanding of the important and often critical functions of protein glycoconjugates. Using innovative interdisciplinary approaches rooted in chemical biology and high resolution mass spectrometry, I will outline our efforts to dismantle the complexity of protein glycoconjugates. These endeavors include the fabrication of defined proteoglycans that regulate mouse embryonic stem cell differentiation, elucidation of the proteome-wide interactions of glycan-binding proteins in liver fibrosis and myogenesis, as well as the development of synthetic small molecules that differentially engage various protein glycoforms.

Taming glycoconjugate structure and interactions in development and disease

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ACS Spring 2023

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