How peptide sequences drive amyloid fiber formation
Official title: Elucidating the sequence code for amyloid peptide self-assembly through all-atom simulations, machine learning, and experiments
Funded at New Jersey Institute of Technology · NIH-11221679 · Data updated 2026-11-12
This project uses detailed computer simulations, machine learning, and lab tests to learn which short protein pieces tend to clump into amyloid fibers linked to Alzheimer's.
Quick facts
| Grant type | R15 grant |
|---|---|
| Study type | NIH-funded research |
| Funding institution | New Jersey Institute of Technology NIH-funded |
| Lab location | 1 site (Newark, United States) |
| Project start | September 22, 2022 |
| Project end | September 1, 2028 |
| Funding year | 2025 |
| Award (this year) | $580,150 |
| NIH project number | 2R15GM148982-02 |
| Project ID | NIH-11221679 on NIH RePORTER |
Who could benefit from this research
✓Could help
There is no patient enrollment expected; the findings are most relevant to people affected by Alzheimer's disease or other amyloid-related conditions who may benefit indirectly from future therapies informed by this work.
✕Less likely to help
People with conditions unrelated to amyloid biology are unlikely to see direct benefit from this project.
What this research studies
From a patient's perspective, researchers will combine atom-by-atom computer simulations, AI, and laboratory experiments to find the sequence patterns that make peptides form amyloid fibrils. They will run all-atom molecular dynamics to observe peptide assembly, train machine-learning models on those results, and validate key predictions with bench experiments. The aim is to create an accessible tool that predicts whether any peptide sequence will form fibrils and to distinguish disease-related amyloids from engineered, non-toxic ones. While this work is basic science, it supports future efforts to design safer biomaterials and to identify targets relevant to Alzheimer's disease.
Why it matters
Potential benefit: If successful, the project could help scientists identify or design peptides less likely to form toxic amyloid deposits, informing future treatments and safer biomaterials.
How similar studies have gone: Recent studies have shown that all-atom simulations can reproduce peptide fibril formation for some systems, but applying these methods broadly to predict any sequence remains a new and expanding effort.
Where this research is happening
-
New Jersey Institute of Technology
Newark, United States Active
Researchers
- Principal investigator: Dias, Cristiano Luis — New Jersey Institute of Technology
- Study coordinator: Dias, Cristiano Luis
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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.