October 21, 2025

Dr. Megna Tiwari’s scientific journey has been anything but linear—beginning as an undergraduate fascinated by biology, continuing through work as a blood bank laboratory technician, and advancing through a master’s, Ph.D., and postdoctoral training.

Her early research focused on infectious agents, but an unexpected encounter with glycobiology sparked a new scientific passion. Captivated by the intricate world of glycans, she began exploring how these small but powerful sugar molecules influence nearly every biological process—a realization she often sums up with the phrase, “From small sugars come big things.”

By the end of her Ph.D., Dr. Tiwari’s curiosity had expanded beyond the lab bench to include the question of how students thrive in science. This led her to combine her love for glycobiology with a growing dedication to science education research.

Now a postdoctoral researcher with Dr. Erin Dolan and the BioF:GREAT team, Dr. Tiwari is helping to democratize glycoscience—developing, testing, and sharing glycoscience teaching materials designed to work across diverse classrooms and learning environments. Her overarching goal is to build national capacity for glycoscience education, ensuring that students and educators alike have access to the tools and knowledge needed to bring this vital field into mainstream biological education.

Visit the education portal

October 16, 2025

Chin Huang, a graduate student in Dr. Kelley Moremen’s BioF:GREAT laboratory, has developed a web-based tool that helps glycan modeling by Alphafold 3.

AlphaFold 3 can accurately model glycans with proper stereochemistry only when using the BAP+CCD syntax, but manually creating these inputs is tedious and error-prone. To streamline the process, JAAG—a lightweight, user-friendly web tool—automates the conversion of glycans drawn by users into BAP+CCD syntax. This makes it easier for scientists to model glycoproteins and glycan–protein interactions, helping even AlphaFold 3 beginners generate reliable, stereochemically valid structures effortlessly.

Use JAAG

• JAAG web tool
• JAAG manuscript (PubMed)
• Tutorial (PDF) and tutorial with animation (PPTX)
• JAAG on this site

February 10, 2024

The University of Georgia’s Complex Carbohydrate Research Center (CCRC) has received an $18 million award from the National Science Foundation (NSF) to advance glycoscience accessibility and research. This funding will support the establishment of the BioFoundry: Glycomaterials Research, Education, and Analysis Training (GREAT), an initiative aiming to democratize the study and application of glycoscience.

Glycans, critical biomolecules found on cell surfaces, play significant roles in cellular communication and biological functions. However, despite their importance alongside nucleic acids, proteins, and lipids, glycoscience remains underrepresented in education and research. The BioFoundry at UGA will aim to change this by providing resources, education, and hands-on training in glycoscience. The facility will give researchers access to advanced tools and training, helping them conduct projects using state-of-the-art technologies like mass spectrometry and nuclear magnetic resonance (NMR) without needing to own such expensive equipment themselves.

Moreover, the initiative will extend its educational impact by offering training and resources across all academic levels, from K-12 to higher education and industry research. The BioFoundry will also offer reduced-cost or free services for clients whose research aligns with the project’s goals, even facilitating short-term training programs in Athens, GA, for eligible researchers.

This effort aligns with the CCRC’s long history of contributions to glycoscience, expanding applications from medical research to biofuel production and plant-based materials.

February 10, 2024

Chondroitin sulfate proteoglycans (CSPGs) play critical roles in various biological functions, particularly in regulating cellular processes in the nervous system. Their structural complexity arises from glycosaminoglycan (GAG) chains attached to core proteins, which makes understanding their structure-function relationships a scientific challenge. Recent advances have been made using solid-phase-supported chemoenzymatic synthesis to address these complexities and provide accurate tools for analysis.

The chemoenzymatic synthesis method employs a combination of solid-phase synthesis techniques and enzymatic modifications to construct glycopeptides that mimic natural CSPGs. This approach allows for precise control over the sulfation patterns and chain lengths of the glycosaminoglycans. Researchers use immobilized peptide resins to streamline the synthesis and ensure efficient enzymatic modification, resulting in a highly defined structure for subsequent analysis.

Advanced analytical techniques, such as nuclear magnetic resonance (NMR) spectroscopy and mass spectrometry, are then used to characterize the synthesized glycopeptides. These methods confirm the structural integrity and provide insight into how different sulfation patterns affect biological activity, such as interactions with proteins or roles in cell signaling.

This solid-phase-supported chemoenzymatic strategy represents a significant advancement in glycoscience. It not only facilitates the production of structurally diverse CSPG mimics but also aids in deciphering the complex biological roles of glycosaminoglycans in processes like neurodevelopment and tissue repair. For more in-depth studies and applications, these methods pave the way for designing novel biomaterials and therapeutic agents targeting CSPG-related functions.

February 10, 2024

O-GlcNAcylation is a dynamic post-translational modification involving the attachment of N-acetylglucosamine (GlcNAc) to serine or threonine residues on nuclear and cytoplasmic proteins. This process serves as a critical nutrient and stress sensor that influences a wide range of cellular functions, impacting processes such as transcription, protein degradation, and cellular signaling pathways.

The dynamic nature of O-GlcNAcylation is maintained through the interplay of two key enzymes: O-GlcNAc transferase (OGT), which adds the GlcNAc moiety, and O-GlcNAcase (OGA), which removes it. Because OGT’s activity is closely linked to cellular metabolic status, O-GlcNAcylation directly reflects changes in nutrient availability, such as fluctuations in glucose and other metabolites derived from the hexosamine biosynthetic pathway.

In response to cellular stress, O-GlcNAcylation often serves as a protective mechanism. During events like heat shock, oxidative stress, or hypoxia, the modification can stabilize proteins, enhance stress response pathways, and regulate the function of key transcription factors. For example, it has been shown to modulate the activity of tumor suppressor p53 and influence the circadian clock by regulating the core clock proteins, thereby linking metabolic cycles with timekeeping mechanisms in the cell.

Given its regulatory role in numerous physiological processes, dysregulation of O-GlcNAcylation has been implicated in various diseases, including diabetes, neurodegenerative disorders, and cancer. Elevated levels of O-GlcNAcylation are often observed in cancer cells, where they may support tumor growth by enhancing cell survival and proliferation. Conversely, reduced O-GlcNAcylation is associated with metabolic disorders like diabetes, underscoring the modification’s role as a metabolic sensor.

Research continues to explore the therapeutic potential of modulating O-GlcNAcylation to treat these conditions, with small molecules targeting OGT or OGA showing promise in preclinical studies. As scientists gain a deeper understanding of how this modification integrates metabolic and stress signals to regulate cellular physiology, it opens new avenues for intervention and the development of metabolic and neuroprotective therapies.