Technology

FIDA stands for Flow Induced Dispersion Analysis: a first-principles, in-solution method that measures molecular size, binding, aggregation and sample quality.

FIDA is based on Taylor Dispersion Analysis and the Stokes–Einstein equation. Together, they make it possible to calculate the absolute hydrodynamic radius of molecules in solution, providing reliable insight into molecular size and interactions. Press to continue reading...

In-solution studies increase data reliability, due to their ability to mimic the natural physiological conditions in which proteins and particles function. Proteins and particles are sensitive structures. Their functions are often impacted by environmental changes, by labelling or by immobilization to a surface structure and functionality of the protein. All-in-all, in-solution studies increase data reliability, due to their ability to mimic the natural physiological conditions in which proteins and particles function. In solution approach allows to better understand the dynamic molecular interactions, conformational changes, and biochemical reactions, leading to more accurate insights into their behavior and enabling the development of more targeted and effective applications in various fields, including drug discovery, diagnostics, and biotechnology. Press to continue reading

FIDA requires a fluorescent signal coming from your sample that can be detected by one of our detectors. It can either be emitting from a label or from the molecule itself, i.e. label-free. The signal coming from your sample that can be detected by one of our detectors: 480, 550, 640, 280. FIDA uses a LED excitation and amplifies the emission signal by PMT. Therefore, FIDA does not use any laser to get a signal, and the sample is not heated. Note that FIDA delivers three orthogonal readouts: absolute size (hydrodynamic radius), fluorescence measurement (Binding Related Intensity Change - BRIC) and Fida Lambda Dynamics, which refers to the measurement of the shifts in the wavelength (lambda) of the detected fluorescence signal, which occurs when binding events change the environment of the fluorophore or other optical markers. Press to continue reading...

FIDA delivers multiple simultaneous readouts, namely: Molecular Size, Sample Viscosity, Sample Stickiness, Binding Kinetics, Quantification, Sample Loss, Binding Affinity, Polydispersity Index, Labelling quality, Aggregation, PDB correlator. This is possible thanks to the absolute character of the hydrodynamic radius measurement FIDA is based on. Press to read more...

Hydrodynamic radius (Rh), is a parameter used to describe the size of a particle or molecule in a fluid, taking into account its shape, mass, and interactions with the surrounding fluid molecules. The hydrodynamic radius is defined as the radius of a hypothetical sphere that diffuses at the same rate as the particle or molecule in question, under the same conditions (Einstein, 1905).

FIDA can measure hydrodynamic sizes with sub-Ångstrøm accuracy. When it comes to size change detection, 5% size change in hydrodynamic radius is a significant assay-window with FIDA. With this level of accuracy, a multitude of applications is opened for a user (binding, confomational changes, unfolding etc.)

Molecular size and molecular weight are the two most used properties to characterise molecules. Molecular size can be approximated with molecular weight. Molecular size refers to the geometry of the molecule and is reported as the hydrodynamic radius (Rh). Rh is the absolute size, in nanometers, of the molecule in solution. On the other hand, molecular weight is calculated as the sum of the atomic weights of all the atoms in a molecule and is reported in kilodaltons (kDa).In general, larger sized molecules tend to have higher molecular weight than smaller molecules, but the relationship between molecular size and weight is not always straightforward. This is especially true when considering different conformational states of proteins, such as globular versus unfolded, as the complexity of measurements increases in this case. Press to keep reading...

No, there is no buffer restriction with FIDA. Hurra! Crude matrix like serum, plasma, fermentation media, cell lysate works perfectly fine on FIDA, which increases clinical relevance of the studies made. On top of that, as the viscosity is measured and compensate at every measurement, high percentage of viscous additive (glycerol, DMSO, PEG…) can be added to your buffer prior a FIDA measurement.

No. Contrary to many other technologies, FIDA provides full buffer flexibility, incl. PEG, Glycerol, DMSO media etc. As the viscosity is measured and compensated at every measurement, a high percentage of viscous additives can be added to your buffer prior to a FIDA measurement.

No, there is none.

Yes, the 96-well plates from FIDA are compatible with pipetting robots

Different binding models are used in the binding curve module in the Fida data analysis software. In general, the binding models are derived assuming that the apparent diffusivity of the indicator is a weighted average of the fractions bound and unbound of the indicator. The exported data can then be treated in generic spreadsheet-based analysis software and custom graphics can be designed for presentations and publications. Press to read more and see calculations.

Yes, Fida Neo can be used to measure kinetics (association kon and dissociation koff rates). It does so in solution, and with no buffer, temperature, detergent or ionic strength constraints.

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The Stokes-Einstein equation written out: every symbol with its SI unit, where the three names come from, and the four conditions it assumes.