# Tailoring Structures of Sulfated Oligosaccharides for Modulating Heparanase Activity

> **NIH NIH R01** · WAYNE STATE UNIVERSITY · 2020 · $240,000

## Abstract

PROJECT SUMMARY
 Within the realm of synthetic carbohydrate chemistry, the stereoselective formation of glycosidic
bonds is of paramount importance. Efficient manipulation of bond connectivity at the anomeric center opens
up new approaches for the synthesis of complex carbohydrates, including the 1,2-cis-2-amino glycosides.
These aminosugars make up one of the most important classes of naturally occurring oligosaccharides and
glyco-conjugates, which play a crucial role as cell-surface receptor ligands for lectins, antibodies, and
enzymes. However, progress toward understanding the specific functions of 1,2-cis-2-aminosugars has been
hampered, due to the formidable challenge of obtaining an adequate supply of well-defined glycosides from
natural sources. In many cases, high purity 1,2-cis-2-aminosugars can only be obtained by chemical
synthesis, which also provides access to structural variants. Although there have been remarkable advances
in the synthesis of 1,2-cis-2-amino glycosides, the disadvantages of current methodologies include the use of
excess activating agents and unpredictable/poor anomeric selectivity.
 In this grant application, our goal is to develop a new and innovative strategy for the effective
synthesis of 1,2-cis-2-amino glycosides via transition metal-catalyzed a-selective glycosylation (Specific
Aim 1). The method that is currently being developed in our group will be broadly applicable and provide
products in high yield and with excellent a-selectivity. The successful completion of the proposed method
would have broad impact in the carbohydrate field, where catalytic methods for stereoselective glycosylation
are still lacking. This transition-metal catalyzed 1,2-cis-2-amino glycosylation methodology will be applied
to the synthesis of bioactive carbohydrate targets, including Campylobcter jejuni N-linked glycan (Specific
Aim 2) which can be used to block Campylobacter jejuni adherence to human gastric epithelial cells and
biding to mammalian lectins, and heparin oligosaccharides which have potent anticoagulant activity and
minimal side effect (Specific Aim 3).
1

## Key facts

- **NIH application ID:** 10134850
- **Project number:** 3R01GM098285-07S1
- **Recipient organization:** WAYNE STATE UNIVERSITY
- **Principal Investigator:** Hien M Nguyen
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2020
- **Award amount:** $240,000
- **Award type:** 3
- **Project period:** 2012-04-01 → 2023-05-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/10134850

## Citation

> US National Institutes of Health, RePORTER application 10134850, Tailoring Structures of Sulfated Oligosaccharides for Modulating Heparanase Activity (3R01GM098285-07S1). Retrieved via AI Analytics 2026-05-27 from https://api.ai-analytics.org/grant/nih/10134850. Licensed CC0.

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