Small Molecule interactions with Membrane Proteins
In-solution characterization of affinity and structural properties of the FcRn IgG1 Fc interaction during product development
Characterising Multivalent Complex Formation Using Controlled Complex Lifetime in Fida 1
Small Molecule Interactions with Membrane Proteins
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
Label-free biophysical assays using nanoliter sample volumes
Technote: The Relationship between hydrodynamic radius and molecular weight
Clone Selection from unpurified samples
Protein Quantification in plasma (probing immune responses in patients)
PDB Correlator Linking Structure and Function
Rapid characterization of LLPS with FIDA
Fully automated characterization of ternary complex formation using flow induced dispersion analysis
High Throughput detergent screening for membrane proteins using nanoliters of sample
Assessment of sample quality with every measurement - Fida 1 Fundamentals
Flow Induced Dispersion Analysis to measure gRNA-Nuclease Interactions for CRISPR-CAS Development
An automated methodology for assesment of protein stability using nanograms of protein
360-degree automated characterization of AAVs: The safe solution for gene therapy
Rapid sizing and characterization of bispecific antibodies
Characterization of Molecular Glues - an automated in-solution platform
Targeted Protein Degradation - Full Characterization of Ternary complexes
Correlating Supramolecular Behaviour in Buffer and Plasma
Screening conformational stability using nanograms of protein
Assessment of Sample Quality with every measurement. FIDA 1 Fundamentals.
Quantification and Characterization of Exosomes
Assessment of protein Stability and Functionality by Flow Induced Dispersion Analysis
Linking Structure and Function: Use PDB data as the baseline for your Fidabio characterisation
Protein Oligomerization: Easy and Accurate determination in plasma and buffer
High throughput detergent screening for membrane proteins
Use of FIDA for rapid characterization of liquid-liquid phase separation
Size-based characterization of peptide-liposome interactions
Easy and Rapid Assessment of Protein ubiquitination, e.g. in PROTAC development
Selective quantification of IgG Directly in F12 Fermentation Media
Functional Characterization of Nanodisc embedded GPCR
Fidabio Clone Selection Assay: Protein Expression Level and affinity directly in fermentation media without purification (Clone Selection from Non-Purified Samples)
Characterization of Conformational Changes by flow induced dispersion analysis
Detection of Auto-Antibodies in Systemic Lupus Erythematosus Patients
Characterizing Multivalent Complex Formation (Agglutination of multivalent antibodies)
360-degree automated characterization of AAVs, safe solution for gene therapy
Rapid Sizing And Characterization of Bispecific Antibodies using nL of Sample
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Applications, Webinars, Posters
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Taylor-dispersion induced phase separation for efficient characterisation of protein condensate formation
Publications
Taylor-dispersion induced phase separation for efficient characterisation of protein condensate formation
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A Benzarone Derivative Inhibits EYA to Suppress Tumor Growth in SHH Medulloblastoma
Publications
A Benzarone Derivative Inhibits EYA to Suppress Tumor Growth in SHH Medulloblastoma
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Applying FIDA for in-solution binding kinetics
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Posters
Applying FIDA for in-solution binding kinetics
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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
Publications
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
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Small Molecule interactions with Membrane Proteins
Posters
Small Molecule interactions with Membrane Proteins
Author Information
Thermodynamic characterization of amyloid polymorphism by microfluidic transient incomplete separation
Publications
Thermodynamic characterization of amyloid polymorphism by microfluidic transient incomplete separation
Author Information
Specific inhibition of α-synuclein oligomer generation and toxicity by the chaperone domain Bri2 BRICHOS
Publications
Specific inhibition of α-synuclein oligomer generation and toxicity by the chaperone domain Bri2 BRICHOS
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Applications of FIDA in Protein Science
Posters
Applications of FIDA in Protein Science
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Immobilization-Free Binding and Affinity Characterization of Higher Order Bispecific Antibody Complexes Using Size-Based Microfluidics
Publications
Immobilization-Free Binding and Affinity Characterization of Higher Order Bispecific Antibody Complexes Using Size-Based Microfluidics
Author Information
Literature
Rapid, Precise Information for Fast and Safe Drug Development
Based on our revolutionary, patented FIDA technology, Fidabio offers rapid, precise information on complex binding interactions and concentration of proteins, particles up to 1,000 nm Dh, antibodies, and other biomolecules.
The core measurements of the FIDA technology, or Flow-Induced-Dispersion- Analysis, are very precise and reproducible, absolute detections of hydrodynamic radii directly in plasma, serum, fermentation media, cell lysate etc. with accuracies of +/- 5 %, coefficient of variations of <5 % and a sensitivity of 0.1 nM FITC type tags. The instrument is fully automated for vials or 2 x 96 wells plates with end-to-end temperature control from 4-55 °C controllable in increments of 0.1 °C. Each test only requires a few hundred nanoliters of sample material.
The FIDA technology provides significant advantages over current technologies in terms of data quality, cost, versatility and time. In other words, Fidabio enables scientists and researchers to carry out tests that are impossible using current technologies leading to faster and safer drug development.
The core measurements of the FIDA technology, or Flow-Induced-Dispersion- Analysis, are very precise and reproducible, absolute detections of hydrodynamic radii directly in plasma, serum, fermentation media, cell lysate etc. with accuracies of +/- 5 %, coefficient of variations of <5 % and a sensitivity of 0.1 nM FITC type tags. The instrument is fully automated for vials or 2 x 96 wells plates with end-to-end temperature control from 4-55 °C controllable in increments of 0.1 °C. Each test only requires a few hundred nanoliters of sample material.
The FIDA technology provides significant advantages over current technologies in terms of data quality, cost, versatility and time. In other words, Fidabio enables scientists and researchers to carry out tests that are impossible using current technologies leading to faster and safer drug development.
Fida 1 Overview
Fida 1 Fundamentals: Assessment of Sample Quality with every measurement
Poster: Assessment of sample quality with every measurement – Fida 1 Fundamentals
Technote: The Relationship between hydrodynamic radius and molecular weight
Analysis of Large Particles
The FIDA technology allows the analysis of proteins and particles 0.5 to 1,000 nm in diameter. This enables analysis of exosomes, liposomes, vaccines, viral vectors, membrane-embedded proteins, intrinsically disordered proteins et. al.
With the Fidabio instrument you can amongst others analyse interactions between targets and membrane proteins and vaccines, characterization of exosomes, liposome and IDPs, quantification of specific exosomes in plasma, quantification of viral vectors in fermentation media etc.
With the Fidabio instrument you can amongst others analyse interactions between targets and membrane proteins and vaccines, characterization of exosomes, liposome and IDPs, quantification of specific exosomes in plasma, quantification of viral vectors in fermentation media etc.
Analysis Directly in Complex Matrices
It is well-known that detection in a buffer, sample preparations and immobilization from time to time impact the data reliability. Detection directly under native conditions ensures you that your decisions are based on the most biologically accurate data.
The FIDA technology is based on in-solution measurements. You can analyze directly in plasma, serum, cell lysate, fermentation media, CHO cells et al. Background noise is eliminated by an automatic adjustment of the baseline and the risk of adsorption is managed with our advanced, proprietary capillary coating.
The FIDA technology is based on in-solution measurements. You can analyze directly in plasma, serum, cell lysate, fermentation media, CHO cells et al. Background noise is eliminated by an automatic adjustment of the baseline and the risk of adsorption is managed with our advanced, proprietary capillary coating.
In-solution Validation Immobilization Data
SPR and BLI are industry standards and are widely used for amongst others affinity Kd determination. Though often robust and reliable, occasionally the surface immobilization might result in difficult-to-interpret artefacts due to mass transport limitations.
With easy setup and validation of new assays and the consumption of only a few hundred nanoliters of sample material, the Fidabio instrument offers a possibility of fast and accurate orthogonal validation of Kd data generated with SPR, BLI etc.
With easy setup and validation of new assays and the consumption of only a few hundred nanoliters of sample material, the Fidabio instrument offers a possibility of fast and accurate orthogonal validation of Kd data generated with SPR, BLI etc.
At Fidabio we support young talents. We help PhDs and Postdocs to make their research visible worldwide.
If you would like to travel to present your research findings file an application for Fidabio Young Scientist Travel Grant.
If you would like to travel to present your research findings file an application for Fidabio Young Scientist Travel Grant.