# NIH grant: Mapping Natural Glycan Interactomes: Investigating Protein-Glycan Interactions in Natural Systems (1R35GM161587-01) — retained record

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NIH grant 1R35GM161587-01: Mapping Natural Glycan Interactomes: Investigating Protein-Glycan Interactions in Natural Systems
Institute: {'code': 'GM', 'abbreviation': 'NIGMS', 'name': 'National Institute of General Medical Sciences', 'admin_org_id': '12500024', 'admin_funding_url': ''}. PI: Xuezheng  Song. Award: $430375.
Start: 2026-08-01T00:00:00.
Project Summary/Abstract
Glycoconjugates, including glycoproteins, glycolipids, and glycosaminoglycans, are fundamental to cellular
communication, immune responses, and molecular recognition. The glycome's complexity and dynamic nature
underscore its importance, yet the field of glycoscience lags behind other areas due to the structural complexity
of glycans and limited analytical tools. In the last two decades, we have dedicated our effort to developing novel
chemistry and tools to remove technical barriers in glycoscience and to facilitate the study of protein-glycan
interactions. This proposal seeks to address these challenges by leveraging and expanding innovative
methodologies developed in our laboratory, including the Oxidative Release of Natural Glycans (ORNG) and
DNA-coded glycan libraries as next-generation glycan microarrays. The ORNG method has revolutionized
glycan extraction, enabling scalable and cost-effective production of diverse natural glycans from biological
sources. This innovation addresses critical bottlenecks in glycoscience, such as the limited availability of complex
glycans for functional studies. Building on this success, our work has advanced preparative glycan separation
techniques, allowing high-purity isolation of glycans at milligram-to-gram scales. These developments are crucial
to many groundbreaking applications in glycoscience, including glycosylation engineering and the synthesis of
glycopeptides and glycoproteins, which are pivotal for studying glycan functions and developing therapeutics.
Looking ahead, our research program aims to deepen the understanding of glycan-mediated processes through
systematic studies of natural glycans and their interactomes. We will expand our natural glycan repertoire by
targeting low-abundance glycans with potentially significant biological functions. This includes developing
advanced enrichment strategies for glycan subclasses such as sialylated, phosphorylated, and sulfated glycans,
which are critical in biological pathways but remain challenging to isolate and synthesize. Additionally, we will
employ these glycans as substrates for enzymatic synthesis, generating structurally diverse libraries that will
support functional and therapeutic studies. A cornerstone of our future work is the application of DNA-coded
glycan libraries to investigate intact cell surface protein-glycan interactomes. Traditional glycan microarrays,
while transformative for studying glycan-protein interactions, are limited in their compatibility with large and
complex biological systems. Our solution-based approach integrates DNA sequencing technologies, enabling
high-throughput, scalable analyses of glycan binding properties on cell surfaces. This technology will be applied
to a range of cell lines, including cancer cells, to uncover glycan ligands that can serve as biomarkers for early
diagnosis, prognosis evaluation, and therapeutic development. By addressing critical challenges in glycan
isolation, enrichment, and functional analysis, our research will advance the field of glycoscience, fostering
discoveries in basic science and translational applications. This comprehensive approach is poised to uncover
novel insights into glycoscience and its implications for health and disease.
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