Chemoenzymatic creation of sulfoglycopeptide libraries to study protein binding
Official title: Chemoenzymatic Synthesis of Libraries of Sulfoglycopeptides
Funded at University of Mississippi · NIH-11330652 · Data updated 2026-11-12
Aims to make diverse, well-defined sulfated and glycosylated peptides to better understand how these chemical tweaks affect protein binding and signaling.
Quick facts
| Grant type | NIH-funded research |
|---|---|
| Study type | NIH-funded research |
| Funding institution | University of Mississippi NIH-funded |
| Lab location | 1 site (University, United States) |
| Project start | July 1, 2024 |
| Project end | May 31, 2029 |
| Funding year | 2026 |
| Award (this year) | $357,646 |
| NIH project number | 5R35GM155126-03 |
| Project ID | NIH-11330652 on NIH RePORTER |
Who could benefit from this research
✓Could help
Ideal participants would be patients with conditions linked to dysregulated protein modification and cell signaling, or those contributing samples for related validation studies.
✕Less likely to help
Some patients may not directly benefit if the work remains at the chemistry and modeling stage without immediate clinical translation.
What this research studies
This project uses synthetic chemistry to build libraries of CSOG-modified peptides and to map how different CSOG structures influence binding and signaling in proteins such as receptors and adhesion molecules. It combines chemistry with computational tools to design, synthesize, and analyze these structure-defined molecules and to develop methods for characterizing CSOG. The work focuses on understanding how precise CSOG patterns tune biological interactions, which could guide future therapeutic or diagnostic efforts. By creating a generalized synthesis strategy, the team aims to enable broader exploration of CSOG’s role across multiple proteins and pathways.
Why it matters
Potential benefit: If successful, the research could enable more precise targeting of protein interactions involved in signaling and adhesion, potentially informing new therapies or diagnostics.
How similar studies have gone: Similar chemistries and computational methods have advanced understanding of PTMs, with meaningful progress in mapping structure–function relationships.
Where this research is happening
-
University of Mississippi
University, United States Active
Researchers
- Principal investigator: Zhu, Hailiang Joshua — University of Mississippi
- Study coordinator: Zhu, Hailiang Joshua
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About this research
- This is an active NIH-funded research project — typically early-stage science, not a clinical trial accepting patient enrollment.
- Some NIH-funded labs run parallel clinical studies or seek volunteers for related work. To check, contact the principal investigator or institution listed above.
- For full project details, budget, and progress reports, visit the official NIH RePORTER page.