How does FIDA move frontiers in amyloid fibril research?
01
Amyloid-fibril Binding Assays:
- Distinguish between binding to monomers, small oligomers and fibrils without any size bias – highly valuable for drug discovery
- Determine the size of fibrils
- Work on patient-derived fibrils (e.g. Cerebral Spinal Fluid)
- Nanoliter to microliter sample sizes
02
Fibril kinetics assay
- Capture data about both presence and size of fibrils
- Monitor development of fibril size over time
- Directly measure size increase over time (unlike THT only measuring appearance)
03
Thermodynamic characterisation of amyloid polymorphism
- Quantify both monomer concentration and fibril concentration in the same assay
- Automated ΔG comparison for diverse polymorphs
- Benefit from a hybrid approach that integrates precision of separation-based techniques with speed of the bulk methods
- Screening of factors influencing fibril stability thanks to temperature control and no pH or saltiness constraints
Technologies Used
ELISA
THT
SEC/SEC-MALS
DLS
CD
CryoEM
AFM
NMR
FIDA
Detection
Sizing
Binding
Kinetics
Structure
Thermodynamics
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Benefits
Distinguish between binding to monomers, small oligomers and fibrils without any size bias
Thermodynamic characterisation of amyloid polymorphism
Monitor the development of fibrils over time
Any pH or ionic strength
Measure the size of amyloid fibrils
Follow the development of fibril growth
Features
Advanced temperature control throughout the analysis
μL of sample consumption for characterisation
nL of sample consumption for screening
Built-in QC
Dedicated software for liquid-liquid phase separation analysis
Automated workflows
Measures
Accurate determination of dilute phase concentration
Relative droplet size distributions
Kinetics of droplet formation and maturation into amyloid fibrils
Determination of binding affinity between the polypeptide undergoing LLPS and LLPS-modulating compounds
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Cellular Protein Chemistry, Bijvoet Centre and Science for Life Utrecht University
"Fida Instrument provides a ''ruler'' to measure the length of fibrils''
Stefan Rüdiger Ph.D.
PROFESSOR OF PROTEIN CHEMISTRY OF DISEASE; HEAD OF DEPARTMENT OF CHEMISTRY
