Accelerating Academic Researchers
FIDA’s value as an academic tool lies in its ability to deliver over 10 key biophysicalparameters with a single technology and in a highly flexible experimental environment.
Multiparametric readouts for more productive research
The multiple readouts allow researchers to gather a wealth of information with one assay—ranging from binding affinities and hydrodynamic radii to concentration and stoichiometry—without the need for multiple instruments, cumbersome assay developments or complex workflows. The iterative FIDA approach significantly reduces the time from hypothesis to validation or rejection. A truly adaptable solution for a wide range of research questions in biophysics.
FIDA technology is grounded in the principles of biophysics, delivering absolute measurements that go beyond mere approximations.
This means that instead of relying on relative comparisons, FIDA directly quantifies critical parameters, giving researchers exact, reproducible data. FIDA ensures that your results are consistent and reliable across different experiments and conditions.
In-Solution Kinetics and Absolute Size
FIDA measures binding kinetics directly in solution, providing a more accurate representation of how molecules behave in their natural state, avoiding the cumbersome workflow of traditional surface-based techniques. The result is precise, easily interpretable, “artefact-free” data on binding affinities and kinetic rates that reflect actual biological conditions. Furthermore, by measuring the absolute size of molecules in solution, FIDA enables monitoring a range of integrity parameters, incl. conformational changes, oligomeric state and protein aggregation—three critical factors influencing drug efficacy and stability.
High Sensitivity Across Concentration Ranges
FIDA excels at measuring interactions across a wide concentration range (pM to mM), fromsmall molecules to large biomolecules. This flexibility is crucial for drug discovery teamswho need to test molecules at varying concentrations without losing sensitivity. Whetherscreening for early hits, optimizing lead compounds, or predicting drug developability, FIDAdelivers the precision needed to confidently assess binding affinity, even in low-concentrationsamples.
Label-Free, Native State Analysis
Traditional methods often require the use of labels or modifications that can interfere with the natural properties of the drug target. With a wide array of detectors available, Fida can operate label-free, preserving the integrity of proteins and other biomolecules. This allows for more reliable data when investigating protein-ligand interactions, which is especially important in the development of biologics where maintaining the natural structure is key
Absolute Data for High-Impact Publications
FIDA delivers absolute, high-quality binding constants, kinetics and interaction data , ensuring reproducibility and accuracy—perfect for peer-reviewed journals and grant applications.
Ease of Use for All Skill Levels
FIDA’s intuitive interface and quick setup mean that even students can master the technology, reducing the training burden on senior researchers and faculty. Furthermore, its clog-free design ensures minimal downtime, meaning your department's research schedule stays on track without costly interruptions.
See our users'
academic publications
Autoantigen TRIM21 (Ro52) assembles pro-1 inflammatory immune complexes following lytic cell death
The mechanism of allosteric activation of SYK kinase derived from multiple phospho-ITAM-bound structures
Peripherally restricted PICK1 inhibitor mPD5 ameliorates pain behaviors in murine inflammatory and neuropathic pain models
Rapid determination of sphingosine 1-phosphate association with carrier molecules by flow induced dispersion analysis to predict sepsis outcome
Fibril Paint: a class of amyloid-targeting peptides
Chaperone BiP controls ER stress sensor Ire1 through interactions with its oligomers
Fibril paint Targets Amyloid Fibrils For Ubiquitination
Avidity within the N-terminal anchor drives α-synuclein membrane interaction and insertion
mPD5, a peripherally restricted PICK1 inhibitor for treating chronic pain
HLA antibody affinity determination: From HLA-specific monoclonal antibodies to donor HLA specific antibodies (DSA) in patient serum
Molecular properties and diagnostic potential of monoclonal antibodies (mAbs) targeting cytotoxic α-synuclein oligomers
Two Receptor Binding Strategy of SARS-CoV-2 is mediated by both the n-terminal and Receptor-binding Spike Domain
TDP-43 is a Master Regulator of Paraspeckle Condensation
Taylor-dispersion induced phase separation for efficient characterisation of protein condensate formation
A Benzarone Derivative Inhibits EYA to Suppress Tumor Growth in SHH Medulloblastoma
Degree of hydrolysis is a poor predictor of the sensitizing capacity of whey- and casein-based hydrolysates in a Brown Norway rat model of cow’s milk allergy
Thermodynamic characterization of amyloid polymorphism by microfluidic transient incomplete separation
Specific inhibition of α-synuclein oligomer generation and toxicity by the chaperone domain Bri2 BRICHOS
Immobilization-Free Binding and Affinity Characterization of Higher Order Bispecific Antibody Complexes Using Size-Based Microfluidics
Drug repurposing screens identify compounds that inhibit α-synuclein oligomers' membrane disruption and block antibody interactions
Fibril Paint to detect Amyloids and determine Fibril Length
Antibodies and α-synuclein: What to target against Parkinson's Disease?
Thermodynamic characterisation of amyloid polymorphism by Taylor dispersion analysis
Taylor-dispersion induced phase separation for the efficient characterisation of protein condensate formation
Flow Induced Dispersion Analysis Quantifies Noncovalent Interactions in Nanoliter Samples
Flow Induced Dispersion Analysis Rapidly Quantifies Proteins in Human Plasma Samples
Flow-Induced Dispersion Analysis for Probing Anti-DsDNA Antibody Binding Heterogeneity in Systemic Lupus Erythematosus Patients
Electromembrane Extraction of Unconjugated Fluorescein Isothiocyanate from Solutions of Labeled Proteins Prior to Flow Induced Dispersion Analysis
Protein Characterization in 3D: Size, Folding, and Functional Assessment in a Unified Approach.
Flow-Induced Dispersion Analysis (FIDA) for Protein Quantification and Characterization
In-Solution IgG Titer Determination in Fermentation Broth Using Affibodies and Flow-Induced Dispersion Analysis.
Size-based characterization of adalimumab and TNF-α interactions using Flow Induced Dispersion Analysis: Assessment of Avidity-stabilized Multiple Bound Species
Biochemical Investigation of the Interaction of pICln, RioK1 and COPR5 with the PRMT5-MEP50 Complex
Microfluidics and the quantification of biomolecular interactions
A serum-stable RNA aptamer specific for SARS-CoV-2 neutralizes viral entry
Capillary flow experiments for thermodynamic and kinetic characterization of protein liquid-liquid phase separation
Bi-directional protein-protein interactions control liquid-liquid phase separation of PSD-95 and its interaction partners
The Protein-Templated Synthesis of Enzyme-Generated Aptamers
Quantification of Structural Integrity and Stability Using Nanograms of Protein by Flow-Induced Dispersion Analysis
Assessment of immunogenicity and drug activity in patient sera by flow-induced dispersion analysis
A lipid transfer protein ensures nematode cuticular impermeability.
Antigen footprint governs activation of the B cell receptor
Generation of Multivalent Nanobody-Based Proteins with Improved Neutralization of Long α-Neurotoxins from Elapid Snakes Bioconjugate
FapA is an Intrinsically Disordered Chaperone for Pseudomonas Functional Amyloid FapC
Generation of robust bispecific antibodies through fusion of single-domain antibodies on IgG scaffolds: a comprehensive comparison of formats
Learn more during an exploratory call with Fidabio team.
We are happy to answer all of your questions. Book an exploratory call to learn more about FIDA and the match between your personal needs and what we can deliver. The call is non-binding and free of any charges, so feel free to fill the form!