Microfluidic Diffusional Sizing (MDS)

A fast and easy method for determining hydrodynamic sizes and interactions of biomolecules in solution

Measure in solution and accelerate progress with MDS

Start quickly, start small

  • No immobilization or purification required – just mix and measure
  • Works for low sample volume

Grab a full picture in 25 mins

  • 25 minutes to data
  • Size, binding affinity (KD), stoichiometry and concentration all at once

Break the barriers

  • No surface constraints
  • Works for any targets and backgrounds

See what really happens without bias

  • No calibration and no prior biophysical knowledge required
  • Quantify binding events in their native state and native environments

How it works

Microfluidic Diffusional Sizing (MDS) measures molecular size (hydrodynamic radius) of a sample by evaluating its diffusion in a microfluidic chamber.

A fluorescently labelled protein enters the microfluidic diffusion chamber together with an auxiliary fluid, in two parallel laminar streams.

The rate of diffusion of protein from one stream to the other depends on the protein’s molecular size.

The rate of diffusion and hydrodynamic radius (Rh) of the protein can be calculated based on the ratio of fluorescence signal detected in the two streams at the end of the chamber.

Changes in size reveal protein interactions

The size of the protein is measured against a titration of binding partner, allowing construction of a binding curve and calculation of binding affinity (KD).

See beyond affinity

The concentration of active binding sites can be determined by measuring binding at different concentrations of the labelled protein. This provides a calibration-free measurement of concentration in complex samples such as biofluids or crude membrane preparations.

Concentration data can also be used to determine binding stoichiometry (number of binding sites per molecule) with the support of the smart assistant Fluidity Insight.

Reach new possibilities

Confidently work with challenging targets and backgrounds that are difficult for traditional methods, because MDS requires no immobilization and purification.

From traditional to challenging targets

  • Globular proteins
  • DNA
  • Antibodies
  • Bispecific antibodies
  • Amyloid fibrils
  • Polyclonal antibodies
  • Disordered proteins
  • PROTACs
  • Membrane proteins

In purified or complex backgrounds

  • Buffers
  • Purified samples
  • Diluted serum and plasma
  • Fermentation broth
  • Saliva
  • Serum and plasma
  • Cell lysate
  • Tissue homogenate
  • Clinical samples

Get ahead in every stage of drug development

MDS enables a wide range of applications throughout different stages of drug development process.

Basic Research

  • Measure binding and activity of your most challenging targets
  • Unlock competition experiments and work with ternary complexes

Drug discovery

  • Validate and characterize hits without having to purify
  • Optimize leads and understand their mechanism of action

Translational Research

  • Obtain concentration and affinity of serum antibodies and overcome limitations imposed by ELISA titers
  • Evaluate immune responses directly in patient samples

Technology comparison

Existing technologies
MDS
Immobilisation of proteins on a surface
  • Non-specific binding
  • Misfolding
  • Avidity effects
In-solution approach
  • Direct use of disease-relevant proteins
  • Native structure
  • No avidity
Purification of proteins
  • Non-native environments
  • Time-consuming
Purification-free workflows
  • Native environments possible
  • Shorter time to result
Indirect measurement principle
  • No in-built assay control
  • Ambiguous results
  • Expert know-how required
Size-based measurement principle
  • In-built assay control
  • Highly reproducible and easy to interpret results
  • Easy for anyone to run
Large sample volumes required
  • Lower number of replicates possible
  • Less material available for complimentary measurements
Small sample volumes
  • More replicates
  • More material available for orthogonal characterization
Slow turnaround
  • Extensive system preparation and lengthy assay development
Quick turnaround
  • Get first data in 25 minutes
One experiment, one parameter
  • Focus on characterizing interactions without learning more about the sample
Binding affinity and beyond
  • Achieve measurements of binding affinity (KD), hydrodynamic radius (Rh) of free probe and protein complex, concentration and stoichiometry
Calibration
  • Dependent on a priori assumption or on empirical calibration
Calibration-free
  • No prior knowledge required. Determine the concentration of active binding sites by measuring binding at different concentrations of the labelled protein

Peer-reviewed publications

    • Highlights
    • Publications

    No data found.

    See MDS in action

    OUR PRODUCT

    Fluidity One-M

    Learn how you can get MDS up and running for your project with the Fluidity One-M system.

    Fluidic Sciences Ltd