Understanding how metal ions trigger transthyretin misfolding and toxic clumps in degenerative diseases
Official title: Mechanistic studies of Metal Ion-Induced Transthyretin Misfolding and Toxic Oligomer Formation
Funded at East Carolina University · NIH-11529960 · Data updated 2026-11-12
This grant looks at how metal ions like zinc and calcium may cause the protein transthyretin to misfold and form harmful clumps that could contribute to conditions like cardiomyopathy and nerve disease.
Quick facts
| Grant type | R15 grant |
|---|---|
| Study type | NIH-funded research |
| Funding institution | East Carolina University NIH-funded |
| Lab location | 1 site (Greenville, United States) |
| Project start | April 1, 2026 |
| Project end | March 31, 2029 |
| Funding year | 2026 |
| Award (this year) | $29,677 |
| NIH project number | 3R15GM163276-01S1 |
| Project ID | NIH-11529960 on NIH RePORTER |
Who could benefit from this research
✓Could help
Patients with transthyretin-related amyloidosis or related degenerative disorders could benefit from future therapies stemming from this research.
✕Less likely to help
This basic science project may not directly involve patients or lead to immediate treatments for individuals who do not have ATTR amyloidosis.
What this research studies
Researchers will study the steps by which normal transthyretin changes shape and forms toxic oligomers in the presence of metal ions. They will use biochemical and structural approaches to map the transition from native protein to misfolded states and identify when and how oligomers emerge. The work aims to uncover the molecular triggers behind misfolding, with the hope of guiding future therapies to prevent pathogenic aggregation. The study is rooted in understanding human disease processes that affect heart and nerve tissues, with potential implications for patients suffering from ATTR amyloidosis.
Why it matters
Potential benefit: Better understanding of how metal ions contribute to harmful protein misfolding could inform new therapies to slow or prevent disease progression in ATTR-related conditions.
How similar studies have gone: Previous work has shown that misfolded transthyretin and oligomer formation are linked to disease, supporting the relevance of this approach.
Where this research is happening
-
East Carolina University
Greenville, United States Active
Researchers
- Principal investigator: Lim, Kwang Hun — East Carolina University
- Study coordinator: Lim, Kwang Hun
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.