Mapping how Alzheimer’s amyloid proteins fold and clump with a new lab method
Mass Spectrometry-Based Protein Footprinting: A New Tool for Amyloid Protein Aggregation
This project uses a mass spectrometry-based technique to map how amyloid beta proteins fold and stick together in Alzheimer’s disease to help people with or at risk for the condition.
Quick facts
| Grant type | R01 grant |
|---|---|
| Study type | NIH-funded research |
| Funding institution | Washington University NIH-funded |
| Lab location | 1 site (Saint Louis, United States) |
| Project ID | NIH-11323571 on NIH RePORTER |
What this research studies
The team will apply protein footprinting coupled with mass spectrometry to measure which parts of the amyloid beta protein are exposed or protected as it changes from single proteins to soluble and insoluble aggregates. They will study how the Alzheimer’s risk protein ApoE (including the ApoE4 form) and cell membrane lipids change amyloid folding and aggregation. The method provides peptide- and amino-acid-level detail about solvent accessibility, dynamics, and binding sites that other techniques cannot easily capture. Results aim to clarify the molecular steps of aggregation that could be used to guide better biomarkers or therapies.
Who could benefit from this research
Good fit: Adults with Alzheimer’s disease, people with mild cognitive impairment, and individuals who carry the APOE-ε4 risk gene would be the most relevant groups for this research.
Not a fit: People with non-amyloid dementias or cognitive problems unrelated to amyloid pathology may not directly benefit from these findings.
Why it matters
Potential benefit: If successful, this work could identify specific molecular steps and sites to block harmful amyloid aggregation, guiding new biomarkers and treatments to slow or prevent Alzheimer’s disease.
How similar studies have performed: Protein footprinting and mass spectrometry have revealed structural details in other protein systems and the investigators have preliminary data, but systematically applying this approach to soluble amyloid intermediates is a novel effort.
Where this research is happening
Saint Louis, United States
- Washington University — Saint Louis, United States (Active)
Researchers
- Principal investigator: Gross, Michael L — Washington University
- Study coordinator: Gross, Michael L
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 below.